Comprehensive Physiology Wiley Online Library

Structure and Function of Membrane Systems of Skeletal Muscle Cells

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Structural Components of Skeletal Muscle Fibers
1.1 Sarcomeres, Striations, and Fibrils
1.2 Membranes
2 Physiological Correlates
2.1 Local Activation Experiments
2.2 Comparison of Slow‐Acting and Fast‐Acting Muscle Fibers
2.3 Relation of Total Surface Area to Fiber Capacitance
2.4 Glycerol‐Shock Experiments
3 Microscopic Methods in Study of Cellular Membrane Structure
3.1 Scanning Electron Microscopy
3.2 High‐Voltage Electron Microscopy of Thick Sections
3.3 Freeze‐Fracture Electron Microscopy
4 T System
4.1 Definition, Development, and Function
4.2 T‐Tubule Networks
4.3 T‐Tubule Shapes
5 Sarcoplasmic Reticulum
5.1 Definition, Development, and Function
5.2 Structural Relationship to Myofibrils and Striations
5.3 Form of Sarcoplasmic Reticulum
5.4 Content of Sarcoplasmic Reticulum
5.5 Calcium Movements
6 Intrinsic Membrane Proteins
6.1 Sarcoplasmic Reticulum
6.2 T Tubules
7 Comparative Structure of Sarcoplasmic Reticulum and T System
7.1 Fibers With One Small Dimension and No T System
7.2 Fibers With Low Speed and Small Quantity of Membranes
7.3 Fibers With High Speed and Large Quantity of Membranes
7.4 Variation in Speed and Quantity of Membranes in Mammalian Fibers
7.5 Invertebrate Fibers
8 T‐System‐Sarcoplasmic Reticulum Couplings
8.1 Basic Form
8.2 Structural Details
8.3 Role of T‐Tubular Calcium Current in Excitation‐ Contraction Coupling
8.4 Functional Mechanism of Coupling Between T Tubules and Sarcoplasmic Reticulum
9 Special Geometry of T System
9.1 Longitudinal T Tubules
9.2 Helicoids
9.3 Structural and Functional Implications
Figure 1. Figure 1.

Bowman 32 was hesitant to accept the fibrillar nature of muscle fibers because the “fibrillae” were so small and thus difficult to separate from one another without “suffering an unnatural mutilation” and because of the difficulties of interpreting optical images of such small objects. He believed, however, that the internal structure of muscle fibers basically is fibrillar. Bowman depicted the fibrils from a macerated ox heart 17 as periodically beaded; this was the basis for his belief that muscle fiber striations are not just on the surface, as van Leeuwenhoek 184 observed earlier, but come from the banded nature of the fibrils inside the fiber. Bowman also depicted a tendency for muscle fibers from a variety of species to disintegrate under certain conditions into transverse disks 21,22,23,24,25,26,27,28,29,30, which led him to challenge van Leeuwenhoek's interpretation of muscle striations as helical. 31, 32, 34: Bowman's view of the sarcolemma in regions where the fiber had broken internally and the fibrillar mass retracted, leaving an empty sarcolemmal tube covering the surface of a muscle fiber. [From Bowman 32.]

Figure 2. Figure 2.

Scanning electron micrograph of portion of a single muscle fiber from frog sartorius muscle. Sarcolemma shows a series of ridges around circumference of fiber. Ridges must be similar to what van Leeuwenhoek observed in his light microscope more than 250 years ago. Satellite cell (S) lies in longitudinal groove in surface of muscle fiber.

Courtesy of R. Mazanet
Figure 3. Figure 3.

High‐voltage electron micrographs of longitudinal sections ∼ 1 μm thick of frog sartorius muscle, lanthanum colloid method. A: low magnification. Surfaces of 2 adjacent muscle fibers pass obliquely through section in this region. Light space between 2 fibers in center of figure shows collagen fibrils. Caveolae in each fiber are filled with dense lanthanum material, making them especially apparent. T tubules also appear dark because of their lanthanum content. 1,000 kV; × 8,400. B: higher magnification and stereo. (Stereoscopic images should be viewed with a simple stereoscope, by diverging the eyes until both images are fused, or by crossing the eyes, in which case front and rear of image will be reversed from description in legends.) Caveolae appear as small, approximately circular structures underlying fibrous connective tissue layer on surface of fiber and plasmalemma and overlying myofibrils. Caveolae groups follow undulations of fiber surface and concentrate in I‐band regions. Arrow, probable connection of T tubule to fiber surface. Total tilt 24°; 1,000 kV; × 12,000.

Figure 4. Figure 4.

A: Emilio Veratti (born in Varese, Italy, Nov. 24, 1872) was a student of medicine at the University of Pavia, where he worked with Camillo Golgi for 5 yr and then spent 1 yr at the University of Bologna, where he obtained his degree (Laurea in Medicina e Chirurgia) in 1896. He was appointed Aiuto of Histology in 1896 and of General Pathology in 1906, both at the University of Pavia. He died in Varese, February 28, 1967, in the same house in which he was born. B: Camillo Golgi, Veratti's professor. Golgi's black‐reaction staining technique, used by Veratti, was recently adapted for use in high‐voltage electron‐microscopic studies of muscle cells 111.

Figure 5. Figure 5.

Phase‐light micrograph of section 1–2 μm. thick prepared using a modification of the Golgi black reaction as used by Veratti. Longitudinal view of long‐sarcomere, tonic‐type muscle fiber from walking leg of crayfish (Astacus fluviatilis). Large regions of extracellular space appear orange. Orange region at lower right, surface of muscle fiber: orange region at upper left, deep infolding or cleft in fiber surface. Smaller clefts enter fiber from surface at right and from large cleft at left. Finer terminations of these smaller clefts tend to lie in a longitudinal position corresponding to Z line of nearby sarcomeres. C, cleft with zigzag profile near micrograph center. Two classes of tubules extend from all fiber surfaces, including those of the clefts. One class is called Z tubulès (Z) because of its sarcomeric location 230. Second class of tubular invaginations from various fiber surfaces is found in 2 sets per sarcomere near ends of A bands (T). Because latter tubules form dyadic associations with sarcoplasmic reticulum (SR), they represent true T tubules of these muscle fibers. Longitudinally oriented tubules (L) connect from individual Z tubules to adjacent T tubules in these muscle fibers, though not as frequently as in some other types of crustacean muscle fibers. × 2,752. (Micrograph by Franzini‐Armstrong, Eastwood, and Peachey.)

Figure 6. Figure 6.

Results of local activation experiments on 3 kinds of muscle fibers by A. F. Huxley and co‐workers 148,150,151,152,244. In actual experiments a single pipette depolarized small patches of surface of an isolated muscle fiber; resulting contractions observed with light microscope. A: frog twitch muscle fibers. Right, contractions obtained only when depolarized patch of membrane is adjacent to Z line of underlying striatum pattern. Left, contraction seen is always symmetric on 2 sides of Z line, even when pipette is displaced to 1 side of Z line. Center, contractions never seen when pipette is over an A band. B: results from local activation experiments on crab muscle fibers 150,152. In these fibers and in lizard fibers, contractions observed only when an area over a region near junction of A bands and I bands was depolarized; resulting contraction always asymmetric and stronger in half I band closer to pipette. Extensive attempts 150 to obtain contractions when a region over Z line and within I band was depolarized gave negative results (center pipette). Extensive longitudinal clefts in sarcolemma of crab fibers; when pipette passes current into these clefts, contractions involving several sarcomeres are seen, regardless of pipette placement with respect to striations. Pipette cannot be considered sealed well enough against fiber surface to restrict depolarization to a small area of membrane. This result shows only that activation can be obtained by depolarization of the membrane within clefts. C: results from local activation experiments on frog slow fibers 244. Fibers behaved quite differently from twitch fibers of same species. Although not all areas of fiber surface led to contraction when depolarized, as was also true with twitch fibers, sensitive spots were found at all levels of the striation pattern in slow fibers. Furthermore, contraction often spread as far longitudinally as radially and thus could involve several sarcomeres. Lack of precise localization of sensitivity and lack of specific spread of activation in the radial direction can be correlated with a similarly imprecise arrangement of T tubules and peripheral couplings in these muscle fibers 222,245.

Figure 7. Figure 7.

T system and SR of frog twitch fiber. Longitudinal axis of fiber is vertical, as drawn. Slightly more than 1 sarcomere length of fiber shown. SR forms a 3–dimensional network of cisternae and tubules around myofibrils, with specific structural differentiation of membrane forms adjacent to specific bands of myofibrillar striations. Two levels of T‐tubular networks shown, adjacent to Z lines within I bands of myofibrils and forming central elements of 3–part structures (triads), which also include 2 SR terminal cisternae (TC). TC of SR connect to SR longitudinal tubules (L) either directly or through SR intermediate cisternae (IC). Near center of A band, longitudinal tubules join fenestrated collar (FC) of SR. [From Peachey 233, by copyright permission of The Rockefeller University Press.]

Figure 8. Figure 8.

Longitudinal section of frog sartorius muscle fiber, seen in thin section in electron microscope. T, T tubules; TC, terminal cisternae; IC, intermediate cisternae; L, longitudinal tubules; FC, fenestrated collar. Glycogen granules (G) intermingled with SR elements between myofibrils. × 23,000.

Figure 9. Figure 9.

Reconstruction of T system of frog twitch muscle fiber made by tracing T tubules stained with peroxidase method in series of high‐voltage electron micrographs of serial transverse sections 0.7 μm thick. T tubules projected into transverse plane of fiber. 1,000 kV; × 1,800. [From Peachey and Eisenberg 240, by copyright permission of the Biophysical Society.]

Figure 10. Figure 10.

Stereoscopic high‐voltage electron micrograph of frog twitch skeletal muscle fiber, Golgi stain. Section 1.5 μm thick. Only T tubules stained in this region. Some artifactual precipitate from stain is found outside T tubules. Nucleus near figure bottom. T‐system networks lie at an oblique angle within thickness of transverse section. Viewed stereoscopically, T tubules do not confine themselves to a flat plane but wander considerably in longitudinal direction of fiber. Total tilt 30°; 1,000 kV; × 6,000. [From Franzini‐Armstrong and Peachey 111; micrograph incorrectly described when originally published.]

Figure 11. Figure 11.

Stereoscopic high‐voltage electron micrograph of frog twitch muscle fiber, Golgi stain. Section 1.5 μm thick. T‐system plane undulates through entire thickness of section within small area represented in micrograph. Total tilt 30°; 1,000 kV; × 5,000.

Figure 12. Figure 12.

Transverse section 0.25–0.5 μm thick of rat white muscle fiber from sternomastoid muscle, Golgi stain. At this thickness, only part of single layer of T system is seen. Clear areas, lipid droplets. 100 kV; × 11,000.

Figure 13. Figure 13.

Transverse section 2.5 μm thick of red muscle fiber from rat sternomastoid muscle, Golgi stain. Two layers of T‐system networks lie within section thickness, resulting in a double image in some regions. Clear areas, lipid droplets, numerous in these red fibers. 1,000 kV; × 9,000.

Figure 14. Figure 14.

Stereoscopic high‐voltage electron micrograph of longitudinal section of tonic, long‐sarcomere muscle fiber from flexor muscle of crayfish leg. Groups of 3 transverse reticula extend transversely across fiber, approximately horizontally. Central of the 3, found at level of Z lines of myofibrils, consists of Z tubules, which do not directly form contacts with SR. Remaining 2 reticula in each sarcomere are T tubules, located near ends of myofibrillar A bands. Occasional longitudinal connections from one network to the next. Section 2 μm thick. Total tilt 14°; 1,000 kV; × 6,000. (Micrograph by Franzini‐Armstrong, Eastwood, and Peachey.)

Figure 15. Figure 15.

Stereoscopic high‐voltage electon micrograph of longitudinal section of phasic muscle fiber from abdominal flexor muscle of crayfish. Only T tubules are seen, forming a network with frequent longitudinal elements and tubules oriented transversely. Section 1 μm thick. Total tilt 30°; 1,000 kV; × 4,000. (Micrograph by Franzini‐Armstrong, Eastwood, and Peachey.)

Figure 16. Figure 16.

Stereoscopic high‐voltage micrograph of transverse section of frog twitch muscle fiber showing 2 forms of T tubules. Flattened ribbonlike tubules predominate, but short segments of round tubules also are seen, especially near nodes in network. Round tubules appear narrower in this transverse view. Section 0.5 μm thick. Total tilt 40°; 1,000 kV; × 10,000.

Figure 17. Figure 17.

Longitudinal section of frog sartorius fiber. Grazing view of SR and T tubules near image center. Terminal cisternae (lateral sacs of triad) face T tubules and contain a dense meshwork of calsequestrin. Intermediate cisternae (arrows) are flat and join lateral sacs to longitudinal tubules. Fenestrated collar opposite sarcomere center. × 45,000.

Figure 18. Figure 18.

Collapsed SR. A: comparison of left, normal SR and right, lumen of SR obliterated. Membranes fuse when portion of SR collapses. B: SR from frog sartorius muscle collapsed with ruthenium red in fixative. Collapsed regions of SR have lost tubular shape, × 43,500. C and D: transverse sections of fibers from frog cutaneous pectoris muscle, frozen rapidly and freeze substituted. Collapse of SR wherever SR membranes have flat shape and SR lumen is obliterated. C, × 42,600; D, × 21,300.

A courtesy of J. Sommer; B from Sommer et al. 307; C and D courtesy of J. Heuser
Figure 19. Figure 19.

Cross sections of frog sartorius fibers at sarcomere center. A: area within A band, except for small area at lower right, in I band. H zone extends vertically in middle of figure. Overlap regions of A band on either side. Transversely cut longitudinal tubules separate myofibrils in overlap region. Fenestrated collar surrounds fibrils opposite H zone, × 31,000. B: most of image occupied by H zone. Pores of fenestrated collar entire SR (arrows) as can be seen at this higher magnification, × 60,000.

Figure 20. Figure 20.

Stereoscopic high‐voltage electron micrograph of Golgi‐stained crab tonic muscle fiber with SR stained. T tubules, stained more densely than SR, show both transversely oriented tubules and flattened disklike regions that form dyad contacts with SR. SR in form of fenestrated cisternae in both A bands and I bands. Section 0.5 μm thick. Total tilt 12°; 1,000 kV; × 6,000. (Micrograph by Franzini‐Armstrong, Eastwood, and Peachey.)

Figure 21. Figure 21.

Golgi‐stained preparation from phasic fiber from crayfish abdominal flexor muscle. Only SR is stained. Numerous flat cisternae of SR match similar regions of T‐tubule network (Fig. 15) with which they form triads and dyads. Fenestrated cisternae of SR less prominent than in tonic fibers. Section 0.5 μm thick. 100 kV; × 15,000. (Micrograph by Franzini‐Armstrong, Eastwood, and Peachey.)

Figure 22. Figure 22.

Freeze‐fractured deep‐etched image of SR in toadfish swimbladder muscle. Between arrows fracture splits interior of lateral sac of triad. Calsequestrin content of cisternae and its connections to SR membrane revealed, × 39,000.

From M. G. Nunzi and C. Franzini‐Armstrong, unpublished observations
Figure 23. Figure 23.

Longitudinal fracture along SR of fish muscle (guppy). Myofilaments barely identifiable in this standard freeze‐fracture image. Membranes very visible (see also Fig. 28). Fracture plane preferentially follows membranes, splitting them into 2 leaflets. Cytoplasmic leaflet (SRC) in SR decorated by uniformly distributed population of small particles of variable size thought to represent aggregates of calcium‐pump proteins. Luminal leaflet (SRL) is smooth. Nonjunctional regions only of T tubules shown; very few particles on either leaflet. × 50,000. [From Franzini‐Armstrong 105.]

Figure 24. Figure 24.

(top left). Detail of cytoplasmic leaflet of SR in frog sartorius fiber. Rotary shadowing allows better visibility of numerous intramembranous particles, × 88,000.

Figure 25. Figure 25.

Transverse section of body musculature of amphioxus. Each flat myofibril (m) forms a muscle fiber, completely covered by plasma membrane (pm). × 26,600. [From Peachey 232, by copyright permission of The Rockefeller University Press.]

Figure 26. Figure 26.

Transverse sections of muscle fiber from superior rectus (extraocular) muscle of domestic cat. Ribbon‐shaped myofibrils and abundant SR arranged in multiple layers between myofibrils, especially in I bands. A, × 20,000; B, × 52,000.

Figure 27. Figure 27.

Longitudinal fracture along fiber from red portion of rat sternomastoid muscle. Location of Z lines (Z) detectable on myofibrils. As in most mammalian fibers, triads (arrows) located at A‐I junction. Extensions of mitochondria (m) encircle myofibrils at I‐band level, immediately adjacent to triads. (See also Fig. 28.) × 25,000.

From R. Mazanet and C. Franzini‐Armstrong, unpublished observations
Figure 28. Figure 28.

Longitudinal thin section of human skeletal muscle showing 2 triads (T) in each sarcomere, large mitochondria (M) in I bands, and large accumulations of glycogen granules (G). × 60,000.

From biopsy material supplied by D. Schotland
Figure 29. Figure 29.

Three views at right angles of junctional feet in triads from toadfish swimbladder. A: grazing view of junction; 2 or 3 parallel rows of feet in tetragonal arrangement, × 36,000. B: section at right angle to long axis of T tubule. Double set of feet covers both flat junctional surfaces of T tubules. × 114,000. C: section approximately parallel to row of feet, showing their periodic arrangement, × 90,000. Feet have different appearances, 2 most frequently illustrated in the literature being a hollow‐cored appearance (arrow, B) and a line parallel to 2 junctional membranes (arrows, C). [C from Franzini‐Armstrong 107.]

Figure 30. Figure 30.

Cytoplasmic leaflets of junctional T‐tubule membrane (A) and plasmalemma at sites of peripheral couplings (B) occupied by similar‐looking large and tall particles. Where most regularly arranged (arrows), particles form groups of 4 separated by twice the distance that separates junctional feet. A: × 74,500; B: × 44,600. [A from Franzini‐Armstrong and Nunzi 109. B from Eastwood, Franzini‐Armstrong, and Peracchia 59.]

Figure 31. Figure 31.

Triad in frog skeletal muscle. Results from both thin sections and freeze‐fracture preparations. [From Franzini‐Armstrong and Nunzi 109.]

Figure 32. Figure 32.

Triads in muscle fibers from frog semitendinosus muscles. A: control untreated with ruthenium red. B and C: muscles treated with ruthenium red after and before glutaraldehyde fixation, respectively. Uptake of ruthenium red by SR and fusion of SR membranes at intermediate cisternae level. A, × 48,000; B, × 94,000; C, × 48,000. [From Howell 142, by copyright permission of the Rockefeller University Press.]

Figure 33. Figure 33.

Stereoscopic high‐voltage electron micrograph of an approximately longitudinal section 3 μm thick of frog sartorius muscle fiber. Lanthanum colloid method used to show T tubules. Several longitudinal connections of T tubules from one network to the next. Left, fiber surface. Total tilt 10°; 1,000 kV; × 10,000.

Figure 34. Figure 34.

Stereoscopic high‐voltage electron micrograph of transverse section of frog muscle fiber, Golgi stain. Region of fiber with helicoid. Almost 2 turns of helicoid within section 5 μm thick. Total tilt 10°; 1,000 kV; × 8,000.

Figure 35. Figure 35.

Stereoscopic high‐voltage electron micrograph of transverse section 3 μm thick from rat white muscle fiber, Golgi stain. Double helicoid with 2 T‐system networks in sarcomere, each completing slightly more than a single turn of the helicoid. Total tilt 16°; 1,000 kV; × 4,000.

Figure 36. Figure 36.

High‐voltage electron micrograph of longitudinal section of frog twitch muscle fiber. Muscle stained with method for SR staining 324, though staining does not show. Displacement of myofibrillar striations occurs, including a vernier displacement between arrows. One more sarcomere between 2 upper arrows than between lower arrows. Section 1 μm thick. 1,000 kV; × 4,000.



Figure 1.

Bowman 32 was hesitant to accept the fibrillar nature of muscle fibers because the “fibrillae” were so small and thus difficult to separate from one another without “suffering an unnatural mutilation” and because of the difficulties of interpreting optical images of such small objects. He believed, however, that the internal structure of muscle fibers basically is fibrillar. Bowman depicted the fibrils from a macerated ox heart 17 as periodically beaded; this was the basis for his belief that muscle fiber striations are not just on the surface, as van Leeuwenhoek 184 observed earlier, but come from the banded nature of the fibrils inside the fiber. Bowman also depicted a tendency for muscle fibers from a variety of species to disintegrate under certain conditions into transverse disks 21,22,23,24,25,26,27,28,29,30, which led him to challenge van Leeuwenhoek's interpretation of muscle striations as helical. 31, 32, 34: Bowman's view of the sarcolemma in regions where the fiber had broken internally and the fibrillar mass retracted, leaving an empty sarcolemmal tube covering the surface of a muscle fiber. [From Bowman 32.]



Figure 2.

Scanning electron micrograph of portion of a single muscle fiber from frog sartorius muscle. Sarcolemma shows a series of ridges around circumference of fiber. Ridges must be similar to what van Leeuwenhoek observed in his light microscope more than 250 years ago. Satellite cell (S) lies in longitudinal groove in surface of muscle fiber.

Courtesy of R. Mazanet


Figure 3.

High‐voltage electron micrographs of longitudinal sections ∼ 1 μm thick of frog sartorius muscle, lanthanum colloid method. A: low magnification. Surfaces of 2 adjacent muscle fibers pass obliquely through section in this region. Light space between 2 fibers in center of figure shows collagen fibrils. Caveolae in each fiber are filled with dense lanthanum material, making them especially apparent. T tubules also appear dark because of their lanthanum content. 1,000 kV; × 8,400. B: higher magnification and stereo. (Stereoscopic images should be viewed with a simple stereoscope, by diverging the eyes until both images are fused, or by crossing the eyes, in which case front and rear of image will be reversed from description in legends.) Caveolae appear as small, approximately circular structures underlying fibrous connective tissue layer on surface of fiber and plasmalemma and overlying myofibrils. Caveolae groups follow undulations of fiber surface and concentrate in I‐band regions. Arrow, probable connection of T tubule to fiber surface. Total tilt 24°; 1,000 kV; × 12,000.



Figure 4.

A: Emilio Veratti (born in Varese, Italy, Nov. 24, 1872) was a student of medicine at the University of Pavia, where he worked with Camillo Golgi for 5 yr and then spent 1 yr at the University of Bologna, where he obtained his degree (Laurea in Medicina e Chirurgia) in 1896. He was appointed Aiuto of Histology in 1896 and of General Pathology in 1906, both at the University of Pavia. He died in Varese, February 28, 1967, in the same house in which he was born. B: Camillo Golgi, Veratti's professor. Golgi's black‐reaction staining technique, used by Veratti, was recently adapted for use in high‐voltage electron‐microscopic studies of muscle cells 111.



Figure 5.

Phase‐light micrograph of section 1–2 μm. thick prepared using a modification of the Golgi black reaction as used by Veratti. Longitudinal view of long‐sarcomere, tonic‐type muscle fiber from walking leg of crayfish (Astacus fluviatilis). Large regions of extracellular space appear orange. Orange region at lower right, surface of muscle fiber: orange region at upper left, deep infolding or cleft in fiber surface. Smaller clefts enter fiber from surface at right and from large cleft at left. Finer terminations of these smaller clefts tend to lie in a longitudinal position corresponding to Z line of nearby sarcomeres. C, cleft with zigzag profile near micrograph center. Two classes of tubules extend from all fiber surfaces, including those of the clefts. One class is called Z tubulès (Z) because of its sarcomeric location 230. Second class of tubular invaginations from various fiber surfaces is found in 2 sets per sarcomere near ends of A bands (T). Because latter tubules form dyadic associations with sarcoplasmic reticulum (SR), they represent true T tubules of these muscle fibers. Longitudinally oriented tubules (L) connect from individual Z tubules to adjacent T tubules in these muscle fibers, though not as frequently as in some other types of crustacean muscle fibers. × 2,752. (Micrograph by Franzini‐Armstrong, Eastwood, and Peachey.)



Figure 6.

Results of local activation experiments on 3 kinds of muscle fibers by A. F. Huxley and co‐workers 148,150,151,152,244. In actual experiments a single pipette depolarized small patches of surface of an isolated muscle fiber; resulting contractions observed with light microscope. A: frog twitch muscle fibers. Right, contractions obtained only when depolarized patch of membrane is adjacent to Z line of underlying striatum pattern. Left, contraction seen is always symmetric on 2 sides of Z line, even when pipette is displaced to 1 side of Z line. Center, contractions never seen when pipette is over an A band. B: results from local activation experiments on crab muscle fibers 150,152. In these fibers and in lizard fibers, contractions observed only when an area over a region near junction of A bands and I bands was depolarized; resulting contraction always asymmetric and stronger in half I band closer to pipette. Extensive attempts 150 to obtain contractions when a region over Z line and within I band was depolarized gave negative results (center pipette). Extensive longitudinal clefts in sarcolemma of crab fibers; when pipette passes current into these clefts, contractions involving several sarcomeres are seen, regardless of pipette placement with respect to striations. Pipette cannot be considered sealed well enough against fiber surface to restrict depolarization to a small area of membrane. This result shows only that activation can be obtained by depolarization of the membrane within clefts. C: results from local activation experiments on frog slow fibers 244. Fibers behaved quite differently from twitch fibers of same species. Although not all areas of fiber surface led to contraction when depolarized, as was also true with twitch fibers, sensitive spots were found at all levels of the striation pattern in slow fibers. Furthermore, contraction often spread as far longitudinally as radially and thus could involve several sarcomeres. Lack of precise localization of sensitivity and lack of specific spread of activation in the radial direction can be correlated with a similarly imprecise arrangement of T tubules and peripheral couplings in these muscle fibers 222,245.



Figure 7.

T system and SR of frog twitch fiber. Longitudinal axis of fiber is vertical, as drawn. Slightly more than 1 sarcomere length of fiber shown. SR forms a 3–dimensional network of cisternae and tubules around myofibrils, with specific structural differentiation of membrane forms adjacent to specific bands of myofibrillar striations. Two levels of T‐tubular networks shown, adjacent to Z lines within I bands of myofibrils and forming central elements of 3–part structures (triads), which also include 2 SR terminal cisternae (TC). TC of SR connect to SR longitudinal tubules (L) either directly or through SR intermediate cisternae (IC). Near center of A band, longitudinal tubules join fenestrated collar (FC) of SR. [From Peachey 233, by copyright permission of The Rockefeller University Press.]



Figure 8.

Longitudinal section of frog sartorius muscle fiber, seen in thin section in electron microscope. T, T tubules; TC, terminal cisternae; IC, intermediate cisternae; L, longitudinal tubules; FC, fenestrated collar. Glycogen granules (G) intermingled with SR elements between myofibrils. × 23,000.



Figure 9.

Reconstruction of T system of frog twitch muscle fiber made by tracing T tubules stained with peroxidase method in series of high‐voltage electron micrographs of serial transverse sections 0.7 μm thick. T tubules projected into transverse plane of fiber. 1,000 kV; × 1,800. [From Peachey and Eisenberg 240, by copyright permission of the Biophysical Society.]



Figure 10.

Stereoscopic high‐voltage electron micrograph of frog twitch skeletal muscle fiber, Golgi stain. Section 1.5 μm thick. Only T tubules stained in this region. Some artifactual precipitate from stain is found outside T tubules. Nucleus near figure bottom. T‐system networks lie at an oblique angle within thickness of transverse section. Viewed stereoscopically, T tubules do not confine themselves to a flat plane but wander considerably in longitudinal direction of fiber. Total tilt 30°; 1,000 kV; × 6,000. [From Franzini‐Armstrong and Peachey 111; micrograph incorrectly described when originally published.]



Figure 11.

Stereoscopic high‐voltage electron micrograph of frog twitch muscle fiber, Golgi stain. Section 1.5 μm thick. T‐system plane undulates through entire thickness of section within small area represented in micrograph. Total tilt 30°; 1,000 kV; × 5,000.



Figure 12.

Transverse section 0.25–0.5 μm thick of rat white muscle fiber from sternomastoid muscle, Golgi stain. At this thickness, only part of single layer of T system is seen. Clear areas, lipid droplets. 100 kV; × 11,000.



Figure 13.

Transverse section 2.5 μm thick of red muscle fiber from rat sternomastoid muscle, Golgi stain. Two layers of T‐system networks lie within section thickness, resulting in a double image in some regions. Clear areas, lipid droplets, numerous in these red fibers. 1,000 kV; × 9,000.



Figure 14.

Stereoscopic high‐voltage electron micrograph of longitudinal section of tonic, long‐sarcomere muscle fiber from flexor muscle of crayfish leg. Groups of 3 transverse reticula extend transversely across fiber, approximately horizontally. Central of the 3, found at level of Z lines of myofibrils, consists of Z tubules, which do not directly form contacts with SR. Remaining 2 reticula in each sarcomere are T tubules, located near ends of myofibrillar A bands. Occasional longitudinal connections from one network to the next. Section 2 μm thick. Total tilt 14°; 1,000 kV; × 6,000. (Micrograph by Franzini‐Armstrong, Eastwood, and Peachey.)



Figure 15.

Stereoscopic high‐voltage electon micrograph of longitudinal section of phasic muscle fiber from abdominal flexor muscle of crayfish. Only T tubules are seen, forming a network with frequent longitudinal elements and tubules oriented transversely. Section 1 μm thick. Total tilt 30°; 1,000 kV; × 4,000. (Micrograph by Franzini‐Armstrong, Eastwood, and Peachey.)



Figure 16.

Stereoscopic high‐voltage micrograph of transverse section of frog twitch muscle fiber showing 2 forms of T tubules. Flattened ribbonlike tubules predominate, but short segments of round tubules also are seen, especially near nodes in network. Round tubules appear narrower in this transverse view. Section 0.5 μm thick. Total tilt 40°; 1,000 kV; × 10,000.



Figure 17.

Longitudinal section of frog sartorius fiber. Grazing view of SR and T tubules near image center. Terminal cisternae (lateral sacs of triad) face T tubules and contain a dense meshwork of calsequestrin. Intermediate cisternae (arrows) are flat and join lateral sacs to longitudinal tubules. Fenestrated collar opposite sarcomere center. × 45,000.



Figure 18.

Collapsed SR. A: comparison of left, normal SR and right, lumen of SR obliterated. Membranes fuse when portion of SR collapses. B: SR from frog sartorius muscle collapsed with ruthenium red in fixative. Collapsed regions of SR have lost tubular shape, × 43,500. C and D: transverse sections of fibers from frog cutaneous pectoris muscle, frozen rapidly and freeze substituted. Collapse of SR wherever SR membranes have flat shape and SR lumen is obliterated. C, × 42,600; D, × 21,300.

A courtesy of J. Sommer; B from Sommer et al. 307; C and D courtesy of J. Heuser


Figure 19.

Cross sections of frog sartorius fibers at sarcomere center. A: area within A band, except for small area at lower right, in I band. H zone extends vertically in middle of figure. Overlap regions of A band on either side. Transversely cut longitudinal tubules separate myofibrils in overlap region. Fenestrated collar surrounds fibrils opposite H zone, × 31,000. B: most of image occupied by H zone. Pores of fenestrated collar entire SR (arrows) as can be seen at this higher magnification, × 60,000.



Figure 20.

Stereoscopic high‐voltage electron micrograph of Golgi‐stained crab tonic muscle fiber with SR stained. T tubules, stained more densely than SR, show both transversely oriented tubules and flattened disklike regions that form dyad contacts with SR. SR in form of fenestrated cisternae in both A bands and I bands. Section 0.5 μm thick. Total tilt 12°; 1,000 kV; × 6,000. (Micrograph by Franzini‐Armstrong, Eastwood, and Peachey.)



Figure 21.

Golgi‐stained preparation from phasic fiber from crayfish abdominal flexor muscle. Only SR is stained. Numerous flat cisternae of SR match similar regions of T‐tubule network (Fig. 15) with which they form triads and dyads. Fenestrated cisternae of SR less prominent than in tonic fibers. Section 0.5 μm thick. 100 kV; × 15,000. (Micrograph by Franzini‐Armstrong, Eastwood, and Peachey.)



Figure 22.

Freeze‐fractured deep‐etched image of SR in toadfish swimbladder muscle. Between arrows fracture splits interior of lateral sac of triad. Calsequestrin content of cisternae and its connections to SR membrane revealed, × 39,000.

From M. G. Nunzi and C. Franzini‐Armstrong, unpublished observations


Figure 23.

Longitudinal fracture along SR of fish muscle (guppy). Myofilaments barely identifiable in this standard freeze‐fracture image. Membranes very visible (see also Fig. 28). Fracture plane preferentially follows membranes, splitting them into 2 leaflets. Cytoplasmic leaflet (SRC) in SR decorated by uniformly distributed population of small particles of variable size thought to represent aggregates of calcium‐pump proteins. Luminal leaflet (SRL) is smooth. Nonjunctional regions only of T tubules shown; very few particles on either leaflet. × 50,000. [From Franzini‐Armstrong 105.]



Figure 24.

(top left). Detail of cytoplasmic leaflet of SR in frog sartorius fiber. Rotary shadowing allows better visibility of numerous intramembranous particles, × 88,000.



Figure 25.

Transverse section of body musculature of amphioxus. Each flat myofibril (m) forms a muscle fiber, completely covered by plasma membrane (pm). × 26,600. [From Peachey 232, by copyright permission of The Rockefeller University Press.]



Figure 26.

Transverse sections of muscle fiber from superior rectus (extraocular) muscle of domestic cat. Ribbon‐shaped myofibrils and abundant SR arranged in multiple layers between myofibrils, especially in I bands. A, × 20,000; B, × 52,000.



Figure 27.

Longitudinal fracture along fiber from red portion of rat sternomastoid muscle. Location of Z lines (Z) detectable on myofibrils. As in most mammalian fibers, triads (arrows) located at A‐I junction. Extensions of mitochondria (m) encircle myofibrils at I‐band level, immediately adjacent to triads. (See also Fig. 28.) × 25,000.

From R. Mazanet and C. Franzini‐Armstrong, unpublished observations


Figure 28.

Longitudinal thin section of human skeletal muscle showing 2 triads (T) in each sarcomere, large mitochondria (M) in I bands, and large accumulations of glycogen granules (G). × 60,000.

From biopsy material supplied by D. Schotland


Figure 29.

Three views at right angles of junctional feet in triads from toadfish swimbladder. A: grazing view of junction; 2 or 3 parallel rows of feet in tetragonal arrangement, × 36,000. B: section at right angle to long axis of T tubule. Double set of feet covers both flat junctional surfaces of T tubules. × 114,000. C: section approximately parallel to row of feet, showing their periodic arrangement, × 90,000. Feet have different appearances, 2 most frequently illustrated in the literature being a hollow‐cored appearance (arrow, B) and a line parallel to 2 junctional membranes (arrows, C). [C from Franzini‐Armstrong 107.]



Figure 30.

Cytoplasmic leaflets of junctional T‐tubule membrane (A) and plasmalemma at sites of peripheral couplings (B) occupied by similar‐looking large and tall particles. Where most regularly arranged (arrows), particles form groups of 4 separated by twice the distance that separates junctional feet. A: × 74,500; B: × 44,600. [A from Franzini‐Armstrong and Nunzi 109. B from Eastwood, Franzini‐Armstrong, and Peracchia 59.]



Figure 31.

Triad in frog skeletal muscle. Results from both thin sections and freeze‐fracture preparations. [From Franzini‐Armstrong and Nunzi 109.]



Figure 32.

Triads in muscle fibers from frog semitendinosus muscles. A: control untreated with ruthenium red. B and C: muscles treated with ruthenium red after and before glutaraldehyde fixation, respectively. Uptake of ruthenium red by SR and fusion of SR membranes at intermediate cisternae level. A, × 48,000; B, × 94,000; C, × 48,000. [From Howell 142, by copyright permission of the Rockefeller University Press.]



Figure 33.

Stereoscopic high‐voltage electron micrograph of an approximately longitudinal section 3 μm thick of frog sartorius muscle fiber. Lanthanum colloid method used to show T tubules. Several longitudinal connections of T tubules from one network to the next. Left, fiber surface. Total tilt 10°; 1,000 kV; × 10,000.



Figure 34.

Stereoscopic high‐voltage electron micrograph of transverse section of frog muscle fiber, Golgi stain. Region of fiber with helicoid. Almost 2 turns of helicoid within section 5 μm thick. Total tilt 10°; 1,000 kV; × 8,000.



Figure 35.

Stereoscopic high‐voltage electron micrograph of transverse section 3 μm thick from rat white muscle fiber, Golgi stain. Double helicoid with 2 T‐system networks in sarcomere, each completing slightly more than a single turn of the helicoid. Total tilt 16°; 1,000 kV; × 4,000.



Figure 36.

High‐voltage electron micrograph of longitudinal section of frog twitch muscle fiber. Muscle stained with method for SR staining 324, though staining does not show. Displacement of myofibrillar striations occurs, including a vernier displacement between arrows. One more sarcomere between 2 upper arrows than between lower arrows. Section 1 μm thick. 1,000 kV; × 4,000.

References
 1. Adrian, R. H. Charge movements in the membrane of striated muscle. Annu. Rev. Biophys. Bioeng. 7: 85–112, 1978.
 2. Adrian, R. H., and W. Almers. Charge movement in the membrane of striated muscle. J. Physiol. London 254: 339–360, 1976.
 3. Adrian, R. H., W. K. Chandler, and R. F. Rakowski. Charge movement and mechanical repriming in striated muscle. J. Physiol. London 254: 361–388, 1976.
 4. Adrian, R. H., and L. D. Peachey. The membrane capacity of frog twitch and slow muscle fibres. J. Physiol. London 181: 324–336, 1965.
 5. Adrian, R. H., and L. D. Peachey. Reconstruction of the action potential of frog sartorius muscle. J. Physiol. London 235: 103–131, 1973.
 6. Adrian, R. H., and A. R. Peres. Charge movement and membrane capacity in frog muscle. J. Physiol. London 289: 83–97, 1979.
 7. Alvarado, J. A., and C. VAN Horn. Muscle cell types of the cat inferior oblique. In: Basic Mechanisms of Ocular Motility and Their Clinical Applications, edited by G. Lennerstrand and P. Bach‐y‐Rita. Oxford, UK: Pergamon, 1975, p. 15–43.
 8. Alvarado‐Mallart, R.‐M. Ultrastructure of muscle fibers of an extraocular muscle of the pigeon. Tissue Cell 4: 327–339, 1972.
 9. Andersson‐Cedergren, E. Ultrastructure of motor end‐plate and sarcoplasmic components of mouse skeletal muscle fiber. J. Ultrastruct. Res. Suppl. 1: 1–191, 1959.
 10. Armstrong, C. M., F. M. Bezanilla, and P. Horowicz. Twitches in the presence of ethylene glycol bis (β‐aminoethyl ether)‐N,N′‐tetraacetic acid. Biochim. Biophys. Acta 267: 605–608, 1972.
 11. Asmussen, G. The properties of the extraocular muscles of the frog. I. Mechanical properties of the isolated superior oblique and superior rectus muscles. Acta Biol. Med. Ger. 37: 301–312, 1978.
 12. Atwood, H. L. Differences in muscle fibre properties as a factor in “fast” and “slow” contraction in Carcinus. Comp. Biochem. Physiol. 10: 17–32, 1963.
 13. Auber, M. Remarques sur l'ultrastructure des myofibrilles chez des scorpions. J. Microsc. Paris 2: 233–236, 1963.
 14. Bach‐Y‐Rita, P. Structural‐functional correlations in eye muscle fibers. Eye muscle proprioception. In: Basic Mechanisms of Ocular Motility and Their Clinical Implications, edited by G. Lennerstrand and P. Bach‐y‐Rita. Oxford, UK: Pergamon, 1975, p. 91–109.
 15. Bach‐Y‐Rita, P., and F. Ito. In vivo studies on fast and slow muscle fibers in cat extraocular muscles. J. Gen. Physiol. 49: 1177–1198, 1966.
 16. Bailey, C. H., and L. D. Peachey. High voltage electron microscopy of the T‐system in slow fibers of the frog cruralis muscle. Annu. Proc. Electron Microsc. Soc. Am., 33rd, Las Vegas, Nevada, 1975, p. 554–555.
 17. Barrett, J. N., and E. F. Barrett. Excitation‐contraction coupling in skeletal muscle: blockade by high extracellular concentration of calcium buffers. Science 200: 1270–1272, 1978.
 18. Baskin, R. J., R. L. Lieber, T. Oba, and Y. Yeh. Intensity of light diffracted from striated muscle as a function of incident angle. Biophys. J. 36: 759–773, 1981.
 19. Baskin, R. J., K. P. Roos, and Y. Yeh. Light diffraction study of single skeletal muscle fibers. Biophys. J. 28: 45–64, 1979.
 20. Baylor, S. M., W. K. Chandler, and M. W. Marshall. Arsenazo III signals in singly dissected frog muscle fibres. (Abstract). J. Physiol. London 287: 23P–24P, 1979.
 21. Beaty, G. N., and E. Stefani. Inward calcium current in twitch muscle fibres of the frog (Abstract). J. Physiol. London 260: 27P–28P, 1976.
 22. Beaty, G. N., and E. Stefani. Calcium dependent electrical activity in twitch muscle fibres of the frog. Proc. R. Soc. London Ser. B 194: 141–150, 1976.
 23. Bennett, G. S., S. A. Fellini, Y. Toyama, and H. Holtzer. Redistribution of intermediate filament subunits during skeletal myogenesis and maturation in vitro. J. Cell Biol. 82: 577–584, 1979.
 24. Bennett, H. S. The structure of striated muscle as seen by the electron microscope. In: The Structure and Function of Muscle (1st ed.), edited by G. H. Bourne. New York: Academic, 1960, vol. 1, p. 137–150.
 25. Bennett, H. S., and K. R. Porter. An electron microscope study of sectioned breast muscle of the domestic fowl. Am. J. Anat. 932: 61–105, 1953.
 26. Berne, R. M. and N. Sperelakis (editors). Handbook of Physiology. Cardiovascular System. Bethesda, MD: Am. Physiol. Soc., 1979, sect. 2, vol. I.
 27. Best, P. M., J. Asayama, and L. E. Ford. Membrane voltage changes associated with calcium movement in skinned muscle fibers. In: Regulation of Muscle Contraction: Excitation‐Contraction Coupling, edited by A. D. Grinnell and M. A. B. Brazier. New York: Academic, 1981, p. 161–170.
 28. Bianchi, C. P., and A. M. Shanes. Calcium influx in skeletal muscle at rest, during activity, and during potassium contracture. J. Gen. Physiol. 42: 803–815, 1959.
 29. Birsk, R. I., and D. F. Davey. Osmotic responses demonstrating the extracellular character of the sarcoplasmic reticulum. J. Physiol. London 202: 171–188, 1969.
 30. Blinks, J. R., R. Rudel, and S. R. Taylor. Calcium transients in isolated amphibian skeletal muscle fibres: detection with aequorin. J. Physiol. London 277: 291–323, 1978.
 31. Bonilla, E. Staining of transverse tubular system of skeletal muscle by tannic acid‐glutaraldehyde fixation. J. Ultrastruct. Res. 58: 162–165, 1977.
 32. Bowman, W. On the minute structure and movements of voluntary muscle. Philos. Trans. R. Soc. London 130: 457–501, 1840.
 33. Brandt, D. E., and C. R. Leeson. Structural differences of fast and slow fibers in human extraocular muscle. Am. J. Ophthalmol. 62: 478–487, 1966.
 34. Brandt, P. N., J. P. Reuben, L. Girardier, and H. Grundfest. Correlated morphological and physiological studies on isolated single muscle fibers. I. Fine structure of the crayfish muscle fiber. J. Cell Biol. 25: 233–260, 1965.
 35. Cajal, S. R. Coloration par la méthode de Golgi des terminaisons des trachées et des nerfs dans les muscles des ailes des insectes. Z. Wiss. Mikrosk. 7: 332–342, 1890.
 36. Campbell, K. P., C. Franzini‐Armstrong, and A. E. Shamoo. Further characterization of light and heavy sarcoplasmic reticulum vesicles. Biochim. Biophys. Acta 602: 97–116, 1980.
 37. Caputo, C. Excitation and contraction processes in muscle. Annu. Rev. Biophys. Bioeng. 7: 63–83, 1978.
 38. Castillo De Maruenda, E., and C. Franzini‐Armstrong. Satellite and invasive cells in frog sartorius muscle. Tissue Cell 10: 749–772, 1978.
 39. Chandler, W. K., R. F. Rakowski, and M. F. Schneider. A non‐linear voltage dependent charge movement in frog skeletal muscle. J. Physiol. London 254: 245–283, 1976.
 40. Chandler, W. K., R. F. Rakowski, and M. F. Schneider. Effects of glycerol treatment and maintained depolarization on charge movement in skeletal muscle. J. Physiol. London 254: 285–316, 1976.
 41. Chiarandini, D. J., and J. Davidowitz. Structure and function of extraocular muscle fibers. In: Current Topics in Eye Research, edited by J. A. Zadunaisky and H. Davson. New York: Academic, 1979, vol. 1, p. 91–142.
 42. Clark, A. W., and E. Schultz. Rattlesnake shaker muscle. II. Fine structure. Tissue Cell 12: 335–351, 1980.
 43. Costantin, L. L. Contractile activation in skeletal muscle. Prog. Biophys. Mol. Biol. 29: 197–224, 1975.
 44. Costantin, L. L. Activation in striated muscle. In: Handbook of Physiology. The Nervous System, edited by J. M. Brookhart and V. B. Mountcastle. Bethesda, MD: Am. Physiol. Soc., 1977, sect. 1, vol. I, pt. 1, chapt. 7, p. 215–259.
 45. Costantin, L. L., and R. J. Podolsky. Depolarization of the internal membrane system in the activation of frog skeletal muscle. J. Gen. Physiol. 50: 1101–1124, 1967.
 46. Costantin, L. L., R. J. Podolsky, and L. W. Tice. Calcium activation of frog slow muscle fibres. J. Physiol. London 188: 261–271, 1967.
 47. Crowe, L. M., and R. J. Baskin. Stereological analysis of developing sarcotubular membranes. J. Ultrastruct. Res. 58: 10–21, 1977.
 48. Crowe, L. M., and R. J. Baskin. Freeze‐fracture of intact sarcotubular membranes. J. Ultrastruct. Res. 62: 147–154, 1978.
 49. Cull‐Candy, S. G., R. Miledi, Y. Nakajima, and O. D. Uchitel. Visualization of satellite cells in living muscle fibres of the frog. Proc. R. Soc. London Ser. B 209: 563–568, 1980.
 50. D'Ancona, U. Per la miglior conoscenza delle terminazione nervose nei muscole somatici dei crostacei decapodi. Trav. Biol. Univ. Madrid 23: 393–423, 1925.
 51. Davidowitz, J., G. Philips, and G. M. Breinin. Organization of the orbital surface layer in rabbit superior rectus. Invest. Ophthalmol. 16: 711–729, 1977.
 52. Davidowitz, J., G. Philips, and G. M. Breinin. Variation of mitochondrial volume fraction along multiply innervated fibers in rabbit extraocular muscle. Tissue Cell 12: 449–457, 1980.
 53. Deamer, D. W., and R. J. Baskin. Ultrastructure of sarcoplasmic reticulum preparations. J. Cell Biol. 42: 269–307, 1969.
 54. Devine, C. E., A. V. Somlyo, and A. P. Somlyo. Sarcoplasmic reticulum and excitation‐contraction coupling in mammalian smooth muscle. J. Cell Biol. 52: 690–718, 1972.
 55. Dewey, M. M., and L. Barr. A study of the structure and distribution of the nexus. J. Cell Biol. 23: 553–585, 1964.
 56. Dulhunty, A. F. The effect of chloride withdrawal on the geometry of the T‐tubules in amphibian and mammalian muscle. J. Membr. Biol. 67: 81–90, 1982.
 57. Dulhunty, A. F., and C. Franzini‐Armstrong. The relative contributions of the folds and caveolae to the surface membrane of frog skeletal muscle fibres at different sarcomere lengths. J. Physiol. London 250: 513–538, 1975.
 58. Dupont, Y., S. C. Harrison, and W. Hasselbach. Molecular organization in the sarcoplasmic reticulum studied by X‐ray diffraction. Nature London 244: 555–558, 1973.
 59. Eastwood, A. B., C. Franzini‐Armstrong, and C. Peracchia. Freeze‐fracture of crustacean muscle. J. Muscle Res. Cell Motil. 3: 273–294, 1982.
 60. Ebashi, S. Excitation contraction coupling. Annu. Rev. Physiol. 38: 293–313, 1976.
 61. Ebashi, S. The Croonian Lecture, 1979. Regulation of muscle contraction. Proc. R. Soc. London Ser. B 207: 259–286, 1980.
 62. Ebashi, S., and M. Endo. Calcium and muscle contraction. Prog. Biophys. Mol. Biol. 18: 123–183, 1968.
 63. Ebashi, S., M. Endo, and I. Ohtsuki. Control of muscle contraction. Q. Rev. Biophys. 2: 351–384, 1969.
 64. Ebashi, S., K. Maruyama, and M. Endo (editors). Muscle Contraction: Its Regulatory Mechanisms. Berlin: Springer‐Verlag, 1980.
 65. Edge, M. B. Development of apposed sarcoplasmic reticulum at the T system and sarcolemma and the change in orientation of triads in rat skeletal muscle. Dev. Biol. 23: 634–659, 1970.
 66. Eisenberg, B. R., and R. S. Eisenberg. Selective disruption of the sarcotubular system in frog sartorius muscle: a quantitative study with exogenous peroxidase as a marker. J. Cell Biol. 39: 451–467, 1968.
 67. Eisenberg, B. R., and R. S. Eisenberg. The T‐SR junction in contracting single skeletal muscle fibers. J. Gen. Physiol. 79: 1–19, 1982.
 68. Eisenberg, B. R., and A. Gilai. Structural changes in single muscle fibers after stimulation at a low frequency. J. Gen. Physiol. 74: 1–16, 1979.
 69. Eisenberg, B. R., R. T. Mathias, and A. Gilai. Intracellular localization of markers within injected or cut frog muscle fibers. Am. J. Physiol. 237 (Celt Physiol. 6): C50–C55, 1979.
 70. Eisenberg, B. R., and L. D. Peachey. The network parameters of the T‐system in frog muscle measured with the high voltage electron microscope. Annu. Proc. Electron Microsc. Soc. Am., 33rd, Las Vegas, Nevada, 1975, p. 550–551.
 71. Eisenberg, R. S. The equivalent circuit of single crab muscle fibers as determined by impedance measurements with intracellular electrodes. J. Gen. Physiol. 50: 1785–1806, 1967.
 72. Eisenberg, R. S., and P. W. Gage. Frog skeletal muscle fibers: changes in electrical properties after disruption of transverse tubular system. Science 158: 1700–1701, 1967.
 73. Endo, M. Entry of fluorescent dyes into the sarcotubular system of frog muscle. J. Physiol. London 185: 224–238, 1964.
 74. Endo, M. Calcium release from the sarcoplasmic reticulum. Physiol. Rev. 57: 71–108, 1977.
 75. Endo, M., and Y. Nakajima. Release of calcium induced by “depolarization” of the sarcoplasmic reticulum membrane. Nature London New Biol. 246: 216–218, 1973.
 76. Engel, A. G. Morphologic and immunopathologic findings in myasthenia gravis and in congenital myasthenic syndrome. J. Neurol. Neurosurg. Psychiatry 43: 577–589, 1980.
 77. Engel, A. G., and R. D. Mcdonald. Ultrastructural reactions in muscle disease and their light microscopic correlates. In: Proc. Int. Congr. Muscle Dis., Milan, 1969. Amsterdam: Excerpta Med., 1969, p. 71–89. (Int. Congr. Ser. No. 199.)
 78. Engel, A. G., T. Santa, and H. H. Stonnington. Morphometric studies of skeletal muscle ultrastructure. Muscle Nerve 2: 229–237, 1979.
 79. Ezerman, E. B., and H. Ishikawa. Differentiation of the sarcoplasmic reticulum and T system in developing chick skeletal muscle in vitro. J. Cell Biol. 35: 405–420, 1967.
 80. Fabiato, A. Myoplasmic free calcium concentration reached during the twitch of an intact isolated cardiac cell and during calcium‐induced release of calcium from the sarcoplasmic reticulum of a skinned cardiac cell from the adult rat or rabbit ventricle. J. Gen. Physiol. 78: 457–497, 1981.
 81. Fabiato, A., and F. Fabiato. Calcium and cardiac excitation‐contraction coupling. Annu. Rev. Physiol. 41: 473–484, 1979.
 82. Fahrenbach, W. H. The sarcoplasmic reticulum of striated muscle of a cyclopoid copepod. J. Cell Biol. 17: 629–640, 1963.
 83. Fahrenbach, W. H. A new configuration of the sarcoplasmic reticulum. J. Cell Biol. 22: 477–481, 1964.
 84. Fahrenbach, W. H. The fine structure of fast and slow crustacean muscle. J. Cell Biol. 35: 69–79, 1967.
 85. Falk, G., and P. Fatt. Linear electrical properties of striated muscle fibres observed with intracellular electrodes. Proc. R. Soc. London Ser. B 160: 69–123, 1964.
 86. Fatt, P. An analysis of the transverse electrical impedance of striated muscle. Proc. R. Soc. London Ser. B 159: 606–651, 1964.
 87. Fatt, P., and B. L. Ginsborg. The ionic requirements for the production of action potentials in crustacean muscle fibres. J. Physiol. London 142: 516–543, 1958.
 88. Fatt, P., and B. Katz. An analysis of the end‐plate potential recorded with an intra‐cellular electrode. J. Physiol. London 115: 320–370, 1951.
 89. Fatt, P., and B. Katz. The electrical properties of crustacean muscle fibres. J. Physiol. London 120: 171–204, 1953.
 90. Fawcett, D. W., and N. S. Mcnutt. The ultrastructure of the cat myocardium. J. Cell Biol. 42: 1–45, 1969.
 91. Fawcett, D. W., and J. P. Revel. The sarcoplasmic reticulum of a fast‐acting fish muscle. J. Biophys. Biochem. Cytol. 1 (4), Suppl.: 89–109, 1961.
 92. Flitney, F. W. The volume of the T‐system and its association with the sarcoplasmic reticulum in slow muscle fibres of the frog. J. Physiol. London 217: 243–257, 1971.
 93. Flood, P. R. Structure of the segmental trunk muscle in amphioxus. With notes on the course and “endings” of the so‐called ventral root fibres. Z. Zellforsch. Mikrosk. Anat. 84: 389–416, 1968.
 94. Flood, P. R. The sarcoplasmic reticulum and associated plasma membrane of trunk muscle lamellae in Branchiostoma lanceolatum (Pallas). A transmission and scanning electron microscopic study including freeze‐fractures, direct replicas and X‐ray microanalysis of calcium oxylate deposits. Cell Tissue Res. 181: 169–196, 1977.
 95. Forbes, M. S., and N. Sperelakis. Myocardial couplings: their structural variations in the mouse. J. Ultrastruct. Res. 58: 50–65, 1977.
 96. Forbes, M. S., and N. Sperelakis. Ruthenium red staining of skeletal and cardiac muscles. Cell Tissue Res. 200: 367–382, 1979.
 97. Forbes, M. S., and N. Sperelakis. Membrane systems in skeletal muscle of the lizard, Anolis carolinensis. J. Ultrastruct. Res. 73: 245–261, 1980.
 98. Ford, L. E., and R. J. Podolsky. Intracellular calcium movements in skinned muscle fibres. J. Physiol. London 223: 21–33, 1972.
 99. Forssmann, W. G., and L. Girardier. A study of the T system in rat heart. J. Cell Biol. 44: 1–19, 1970.
 100. Franzini‐Armstrong, C. Studies of the triad. I. Structure of the junction in frog twitch fibers. J. Cell Biol. 47: 488–499, 1970.
 101. Franzini‐Armstrong, C. Studies of the triad. II. Penetration of tracer into the junctional gap. J. Cell Biol. 49: 196–203, 1971.
 102. Franzini‐Armstrong, C. Studies of the triad. IV. Structure of the junction in frog slow fibers. J. Cell Biol. 56: 120–128, 1973.
 103. Franzini‐Armstrong, C. Membranous systems in muscle fibers. In: The Structure and Function of Muscle (2nd ed.) edited by G. H. Bourne. New York: Academic, 1973, vol. 2, p. 531–619.
 104. Franzini‐Armstrong, G. Freeze‐fracture of striated muscle from a spider. Structural differentiations of sarcoplasmic reticulum and transverse tubular membranes. J. Cell Biol. 61: 501–520, 1974.
 105. Franzini‐Armstrong, C. Membrane particles and transmission at the triad. Federation Proc. 34: 1382–1389, 1975.
 106. Franzini‐Armstrong, C. The comparative structure of intracellular junctions in striated muscle fibers. In: Pathogenesis of Muscular Dystrophies, Proc. Int. Conf. Muscular Dystrophy Assoc., 5th, Durango, Colorado, June 21–25, 1976, p. 612–625.
 107. Franzini‐Armstrong, C. Structure of the sarcoplasmic reticulum. Federation Proc. 39: 2403–2409, 1980.
 108. Franzini‐Armstrong, C., A. B. Eastwood, and L. D. Peachey. A new view of Veratti's “reticulum” in crustacean muscle fibers (Abstract). J. Cell Biol. 79: 330a, 1978.
 109. Franzini‐Armstrong, C., and G. Nunzi. Junctional feet and particles in the triads of a fast twitch muscle fiber. J. Muscle Res. Cell Motil. In press.
 110. Franzini‐Armstrong, C., and L. D. Peachey. Striated muscle—contractile and control mechanisms. J. Cell Biol. 91: looses, 1981.
 111. Franzini‐Armstrong, C., and L. D. Peachey. A modified Golgi black reaction method for light and electron microscopy. J. Histochem. Cytochem. 30: 99–105, 1982.
 112. Franzini‐Armstrong, C., and K. R. Porter. Sarcolemmal invaginations constituting the T‐system in fish muscle fibers. J. Cell Biol. 22: 675–696, 1964.
 113. Fujino, M., T. Yamaguchi, and K. Suzuki. Glycerol effect and the mechanism linking excitation of the plasma membrane with contraction. Nature London 192: 1159–1161, 1961.
 114. Gilai, A., and I. Parnas. Electromechanical coupling in tubular muscle fibers. I. The organization of tubular muscle fibers in the scorpion Leiurus quinquestriatus. J. Cell Biol. 52: 626–638, 1972.
 115. Gillis, J. M., A. Piront, and C. Gosselin‐Rey. Parvalbumins. Distribution and physical state inside the muscle cell. Biochim. Biophys. Acta 585: 444–450, 1979.
 116. Gilly, W. F., and C. S. Hui. Mechanical activation in slow and twitch skeletal muscle fibres of the frog. J. Physiol. London 301: 137–156, 1980.
 117. Gilly, W. F., and C. S. Hui. Membrane electrical properties of frog slow muscle fibres. J. Physiol. London 301: 157–173, 1980.
 118. Gilly, W. F., and C. S. Hui. Voltage‐dependent charge movement in frog slow muscle fibres. J. Physiol. London 301: 175–190, 1980.
 119. Goldstein, M. A. A morphological and cytochemical study of sarcoplasmic reticulum and T system of fish extraocular muscle. Z. Zellforsch. Mikrosk. Anat. 102: 31–39, 1969.
 120. Goldstein, M. A. Anionic binding of ruthenium red in fish extraocular muscle. Z. Zellforsch. Mikrosk. Anat. 102: 459–465, 1969.
 121. Gordon, A. M., A. F. Huxley, and F. J. Julian. The variation of isometric tension with sarcomere length in vertebrate muscle fibres. J. Physiol. London 184: 170–192, 1966.
 122. Gosselin‐Rey, C., and C. Gerday. Parvalbumins from frog skeletal muscle (Rana temporaria L.); isolation and characterization; structural modifications associated with calcium binding. Biochem. Biophys. Acta 492: 53–63, 1977.
 123. Graham, R. C., and M. J. Karnovsky. The early stages of absorption of injected horseradish peroxidase in the proximal tubules of mouse kidney: ultrastructural cytochemistry by a new technique. J. Histochem. Cytochem. 14: 291–302, 1966.
 124. Grenacher, H. Beiträge zur nähern Kenntniss der Muskulatur der Cyclostoma und Leptocardier. Z. Wiss. Zool. 17: 577–597, 1867.
 125. Grinnell, A. D. and M. A. Brazier (editors). The Regulation of Muscle Contraction: Excitation‐Contraction Coupling. New York: Academic, 1981.
 126. Gupta, B. L., and T. A. Hall. The X‐ray microanalysis of frozen‐hydrated sections in scanning electron microscopy. Tissue Cell 13: 623–643, 1981.
 127. Hagiwara, S., M. P. Henkart, and Y. Kidokoro. Excitation contraction coupling in amphioxus muscle cells. J. Physiol. London 219: 233–251, 1971.
 128. Hagopian, M., and D. Spiro. The sarcoplasmic reticulum and its association with the T system in an insect. J. Cell Biol. 32: 535–545, 1967.
 129. Haiech, J., J. Derancourt, and J. G. Demaille. Magnesium and calcium binding to parvalbumins: evidence for differences between parvalbumins and an explanation of their relaxing function. Biochemistry 13: 2752–2758, 1979.
 130. Hamoir, G., and B. Focant. Proteinic differences between the sarcoplasmic reticulums of the superfast swimbladder and the fast skeletal muscles of the toadfish Opsanus tau. Mol. Physiol. 1: 353–359, 1981.
 131. Harris, E. J. Distribution and movement of muscle chloride. J. Physiol. London 166: 87–109, 1963.
 132. Herbette, L., J. Morquart, A. Scarpa, and J. K. Blasie. A direct analysis of lamellar X‐ray diffraction from hydrated oriented multilayers of fully‐functional sarcoplasmic reticulum. Biophys. J. 20: 245–272, 1977.
 133. Hess, A. The structure of slow and fast extrafusal muscle fibers in the extraocular muscles and their nerve endings in guinea pigs. J. Cell. Comp. Physiol. 58: 63–79, 1961.
 134. Hess, A., and G. Pilar. Slow fibres in the extraocular muscles of the cat. J. Physiol. London 169: 780–798, 1963.
 135. Hidalgo, C., and N. Ikemoto. Disposition of proteins and amino phospholipids in the sarcoplasmic reticulum membrane. J. Biol. Chem. 252: 8446–8454, 1977.
 136. Hill, A. V. On the time required for diffusion and its relation to processes in muscle. Proc. R. Soc. London Ser. B 135: 446–453, 1948.
 137. Hill, A. V. The abrupt transition from rest to activity in muscle. Proc. R. Soc: London Ser. B 136: 399–420, 1949.
 138. Hodgkin, A. L., and P. Horowicz. The effect of sudden changes in ionic concentrations on the membrane potential of single muscle fibres. J. Physiol. London 153: 370–385, 1960.
 139. Horowicz, P., and M. F. Schneider. Membrane charge movement in contracting and non‐contracting skeletal muscle fibres. J. Physiol. London 314: 565–593, 1981.
 140. Horowicz, P., and M. F. Schneider. Membrane charge moved at contraction thresholds in skeletal muscle fibres. J. Physiol. London 314: 595–633, 1981.
 141. Howell, J. N. A lesion of the transverse tubules of skeletal muscle. J. Physiol. London 201: 515–533, 1969.
 142. Howell, J. N. Intracellular binding of ruthenium red in frog skeletal muscle. J. Cell Biol. 62: 242–247, 1974.
 143. Howell, J. N., and D. J. Jenden. T‐tubules of skeletal muscle: morphological alterations which interrupt excitation‐contraction coupling (Abstract). Federation Proc. 26: 553a, 1967.
 144. Hoyle, G. Comparative aspects of muscle. Annu. Rev. Physiol. 31: 43–84, 1969.
 145. Hoyle, G., P. A. Mcneill, and A. I. Selverston. Ultrastructure of barnacle giant muscle fibers. J. Cell Biol. 56: 74–91, 1973.
 146. Hoyle, G., P. A. Mcneill, and B. Walcott. Nature of invaginating tubules in Felderstruktur muscle fibers of the garter snake. J. Cell Biol. 30: 197–201, 1966.
 147. Hutchinson, T. E. Determination of subcellular elemental composition through ultrahigh resolution electron microprobe analysis. Int. Rev. Cytol. 58: 115–158, 1979.
 148. Huxley, A. F. The Croonian Lecture, 1967. The activation of striated muscle and its mechanical response. Proc. R. Soc. London Ser. B 178: 1–27, 1971.
 149. Huxley, A. F. Looking back on muscle. In: The Pursuit of Nature, edited by A. L. Hodgkin, et al. Cambridge, UK: Cambridge Univ. Press, 1977, p. 23–64.
 150. Huxley, A. F., and L. D. Peachey. Local activation of crab muscle (Abstract). J. Cell Biol. 23: 107A, 1964.
 151. Huxley, A. F., and R. E. Taylor. Function of Krause's membrane (Abstract). Nature London 176: 1068, 1955.
 152. Huxley, A. F., and R. E. Taylor. Local activation of striated muscle fibres. J. Physiol. London 144: 426–441, 1958.
 153. Huxley, H. E. Evidence for continuity between the central elements of the triads and extracellular space in frog sartorius muscle. Nature London 202: 1067–1071, 1964.
 154. Huxley, H. E., S. Page, and D. R. Wilkie. An electron microscopic study of muscle in hypertonic solutions (Appendix to M. Dydynska and D. R. Wilkie). J. Physiol. London 169: 312–329, 1963.
 155. Ildeponse, M., J. Pager, and O. Rougier. Analyse des propriétés de rectification de la fibre musculaire squelettique rapides aprés traitement au Glycerol. C. R. Acad. Sci. Paris 268: 2783–2786, 1969.
 156. Ishikawa, H. Formation of elaborate networks of T‐system tubules in cultured skeletal muscle with special reference to the T‐system formation. J. Cell Biol. 38: 51–66, 1968.
 157. Ishikawa, H., Y. Fukuda, and E. Yamada. Freeze‐replica observations on frog sartorius muscle. I. Sarcolemmal specializations. J. Electron Microsc. 24: 97–107, 1975.
 158. Ishikawa, H., and E. Yamada. Differentiation of the sarcoplasmic reticulum and T‐system in developing mouse cardiac muscle . In: Developmental and Physiological Correlates of Cardiac Muscle, edited by M. Lieberman and T. Sano. New York: Raven, 1971, p. 21–35.
 159. Jahromi, S. S., and H. L. Atwood. Correlation of structure, speed of contraction and total tension in fast and slow abdominal muscles of the lobster (Homarus americanus). J. Exp. Zool. 171: 25–38, 1969.
 160. Jasper, D. Body muscles of the lamprey: some structural features of the T system and sarcolemma. J. Cell Biol. 32: 219–227, 1967.
 161. Jewett, P. H., J. R. Sommer, and E. A. Johnson. Cardiac muscle. Its ultrastructure in the finch and hummingbird with special reference to the sarcoplasmic reticulum. J. Cell Biol. 49: 50–65, 1971.
 162. Johnson, E. A., and J. R. Sommer. A strand of cardiac muscle. Its ultrastructure and the electrophysiological implications of its geometry. J. Cell Biol. 33: 103–129, 1967.
 163. Jorgensen, A. O., V. Kalnins, and D. H. Maclennan. Localization of sarcoplasmic reticulum proteins in rat skeletal muscle by immunofluorescence. J. Cell Biol. 80: 372–384, 1979.
 164. Jorgensen, A. O., A. C. Y. Shen, D. H. Maclennan, and K. T. Tokuyashi. Ultrastructural localization of the Ca2+ + Mg2+‐dependent ATPase of sarcoplasmic reticulum in rat skeletal muscle by immunoferritin labeling of ultrathin frozen sections. J. Cell Biol. 92: 409–416, 1982.
 165. Judy, M. M., V. Summerour, T. Leconey, R. L. Roa, and G. H. Templeton. Muscle diffraction theory. Relationship between diffraction subpeaks and discrete sarcomere length distributions. Biophys. J. 37: 475–487, 1982.
 166. Karp, R., J. C. Silcox, and A. V. Somlyo. Cryoultramicrotomy: evidence against melting and the use of a low temperature cement for specimen preparation. J. Microsc. 125: 157–165, 1982.
 167. Katz, B. The electrical properties of the muscle fibre membrane. Proc. R. Soc. London Ser. B 135: 506–534, 1948.
 168. Kelly, A. M. Myofibrillogenesis and Z‐band differentiation. Anat. Rec. 163: 403–426, 1968.
 169. Kelly, A. M. Sarcoplasmic reticulum and T‐tubules in differentiating rat skeletal muscle. J. Cell Biol. 49: 335–344, 1971.
 170. Kelly, A. M. T tubules in neonatal rat soleus and extensor digitorum longus muscles. Dev. Biol. 80: 501–505, 1980.
 171. Kelly, D. E. The fine structure of skeletal muscle triad junctions. J. Ultrastruct. Res. 29: 37–49, 1969.
 172. Kelly, D. E., and A. M. Kuda. Subunits of triadic junctions in fast skeletal muscle as revealed by freeze‐fracture. J. Ultrastruct. Res. 68: 220–233, 1979.
 173. Kovacs, L., E. Rios, and M. F. Schneider. Calcium transients and intramembrane charge movements in skeletal muscle fibers. Nature London 279: 391–396, 1979.
 174. Krolenko, S. A. Changes in the T system of muscle fibers under the influence of influx and efflux of glycerol. Nature London 221: 966–968, 1969.
 175. Krüger, P. Tetanus und Tonus der guergestreiften Skeletmuskeln der Wirbeltiere und des Menschen. Leipzig, East Germany: Akad. Verlagsgesellschaft, 1952.
 176. Kulczycky, S., and G. W. Mainwood. Evidence for a functional connection between the sarcoplasmic reticulum and the extracellular space in frog sartorius muscle. Can. J. Physiol. Pharmacol. 50: 87–89, 1972.
 177. LÄNnergren, J. Structure and function of twitch and slow fibers in amphibian skeletal muscle. In: Basic Mechanisms of Ocular Motility and Their Clinical Implications, edited by G. Lennerstrand and P. Bach‐y‐Rita. New York: Pergammon, 1975, p. 63–84.
 178. Lau, Y. H., A. H. Caswell, and J. P. Brunschwig. Isolation of transverse tubules by fractionation of triad junctions of skeletal muscle. J. Biol. Chem. 252: 5565–5574, 1977.
 179. Lau, Y. H., A. H. Caswell, J. P. Brunschwig, R. J. Baerwald, and M. Garcia. Lipid analysis and freeze‐fracture studies on isolated transverse tubules and sarcoplasmic reticulum fractions of skeletal muscle. J. Biol. Chem. 254: 540–546, 1979.
 180. Lavallard, R. Estudo com o microscópio eletrônico do retículo endoplasmático em fibras musculares de carangueijos. São Paulo, Brazil: Univ. of São Paulo, 1960, Bull. 260, Zool. 23, p. 141–169.
 181. Lazarides, E. The distribution of desmin (100 Å) filaments in primary cultures of embryonic chick cardiac cells. Exp. Cell Res. 112: 265–273, 1978.
 182. Lazarides, E. Intermediate filaments as mechanical integrators of cellular space. Nature London 283: 249–256, 1980.
 183. Lazarides, E., and B. H. Hubbard. Immunological characterization of the subunit of 100 Å filaments from muscle cells. Proc. Natl. Acad. Sci. USA 73: 4344–4348, 1976.
 184. Lechene, C. Electron probe microanalysis of biological soft tissues: principles and technique. Federation Proc. 39: 2871–2880, 1980.
 185. VAN Leeuwenhoek, A. A letter from Mr. Anthony van Leeuwenhoek, F.R.S. Containing his observations upon the seminal vesicles, muscular fibres, and blood of whales. Philos. Trans. R. Soc. London Ser. B 27: 438–446, 1712.
 186. Luff, A. R., and H. L. Atwood. Changes in the sarcoplasmic reticulum and transverse tubular system of fast and slow skeletal muscles of the mouse during postnatal development. J. Cell Biol. 51: 369–383, 1971.
 187. Luft, J. H. Fine structure of nerve and muscle cell membrane: permeability to ruthenium red. Anat. Rec. 154: 379–380, 1966.
 188. Luft, J. H. Ruthenium red and violet. II. Fine structural localization in animal tissues. Anat. Rec. 171: 369–415, 1971.
 189. LÜTtgau, H. C., and W. Spiecker. The effects of calcium deprivation upon mechanical and electrophysiological parameters in skeletal muscle fibres of the frog. J. Physiol. London 296: 411–429, 1979.
 190. Maclennan, D. H. Purification and properties of an adenosinetriphosphatase from the sarcoplasmic reticulum. J. Biol. Chem. 245: 4508–4518, 1970.
 191. Maclennan, D. H., and P. C. Holland. Calcium transport in sarcoplasmic reticulum. Annu. Rev. Biophys. Bioeng. 4: 377–404, 1975.
 192. Maclennan, D. H., and P. T. S. Wong. Isolation of a calcium‐sequestering protein from sarcoplasmic reticulum. Proc. Natl. Acad. Sci. USA 68: 1231–1235, 1971.
 193. Martonosi, A., D. Roupa, E. Reyes, and T. W. Tillack. Development of sarcoplasmic reticulum in cultured chicken muscle. J. Biol. Chem. 252: 318–332, 1977.
 194. Mathias, R. T. An analysis of the electrical properties of a skeletal muscle fiber containing a helicoidal T system. Biophys. J. 23: 277–284, 1978.
 195. Mathias, R. T., R. A. Levis, and R. S. Eisenberg. Electrical models of excitation‐contraction coupling and charge movement in skeletal muscle. J. Gen. Physiol. 76: 1–31, 1980.
 196. Matyushkin, D. P., and T. M. Drabkina. Electrophysiological characteristics of tonic fibers of the extrinsic ocular muscles. Fiziol. Zh. SSSR im. I.M. Sechenova 56: 563–569, 1970.
 197. Mauro, A. (editor). Muscle Regeneration. New York: Raven, 1979.
 198. Mauro, A., and W. R. Adams. The structure of the sarcolemma of the frog skeletal muscle fiber. J. Biophys. Biochem. Cytol. 10 (4), Suppl.: 177–185, 1961.
 199. Mayr, R. Structure and distribution of fibre types in the external eye muscles of the rat. Tissue Cell 3: 433–462, 1971.
 200. Mazanet, R., B. F. Reese, C. Franzini‐Armstrong, and T. S. Reese. Variability in the shapes of satellite cells in normal and injured frog sartorius muscle. Dev. Biol. 93: 22–27, 1982.
 201. Mccallister, L. P., and R. Hadek. Transmission electron microscopy and stereo ultrastructure of the T system in frog skeletal muscle. J. Ultrastruct. Res. 33: 360–368, 1970.
 202. Meis, L. DE. The Sarcoplasmic Reticulum. Transport and Energy Transduction. New York: Wiley, 1981.
 203. Meissner, G. Isolation and characterization of two types of sarcoplasmic reticulum vesicles. Biochim. Biophys. Acta 389: 51–68, 1975.
 204. Melzer, W. Die Activierung der Myotome von Branchiostoma lanceolatum. Bochum, West Germany: Ruhr‐Universität Bochum, 1980. Dissertation.
 205. Miledi, R., E. Parker, and G. Schalow. Calcium transients in frog slow muscle fibres. Nature London 268: 750–752, 1977.
 206. Miledi, R., E. Parker, and G. Schalow. Measurement of calcium transients in frog muscle by the use of arsenazo III. Proc. R. Soc. London Ser. B 198: 201–210, 1977.
 207. Miledi, R., E. Parker, and G. Schalow. Calcium transients in normal and denervated slow muscle fibres of the frog. J. Physiol. London 318: 191–206, 1981.
 208. Miller, J. E. Cellular organization of Rhesus extraocular muscle. Invest. Ophthalmol. 6: 18–39, 1967.
 209. Millman, B. M., and P. M. Bennett. Structure of the cross‐striated adductor muscle of the scallop. J. Mol. Biol. 102: 439–467, 1976.
 210. Mobley, B. A., and G. Eidt. Transverse impedance of single frog skeletal muscle fibers. Biophys. J. 40: 51–59, 1982.
 211. Mobley, B. A., and B. R. Eisenberg. Sizes of components in frog skeletal muscle measured by methods of stereology. J. Gen. Physiol. 66: 31–45, 1975.
 212. Morad, M. (editor). Biophysical Aspects of Cardiac Muscle. New York: Academic, 1978.
 213. Nakajima, S., Y. Nakajima, and L. D. Peachey. Speed of repolarization and morphology of glycerol‐treated frog muscle fibres. J. Physiol. London 234: 465–480, 1973.
 214. Nelson, D. A., and E. S. Benson. On the structural continuities of the transverse tubular system of rabbit and human myocardial cells. J. Cell Biol. 16: 217–313, 1963.
 215. Neville, M. C. The extracellular compartments of frog skeletal muscle. J. Physiol. London 288: 45–70, 1979.
 216. Niedergerke, R. Movements of Ca in frog heart ventricles at rest and during contractures. J. Physiol. London 167: 515–550, 1963.
 217. Niedergerke, R., and R. K. Orkand. The dual effect of calcium on the action potential of the frog's heart. J. Physiol. London 184: 291–311, 1966.
 218. Nunzi, M. G., and C. Franzini‐Armstrong. Trabecular network in adult skeletal muscle. J. Ultrastruct. Res. 73: 21–26, 1980.
 219. Nunzi, M. G., and C. Franzini‐Armstrong. The structure of smooth and striated portions of the adductor muscle of the valves in a scallop. J. Ultrastruct. Res. 76: 134–148, 1981.
 220. Oetliker, H. An appraisal of the evidence for a sarcoplasmic reticulum membrane potential and its relation to calcium release in skeletal muscle. J. Muscle Res. Cell Motil. 3: 247–272, 1982.
 221. Page, S. G. The organization of the sarcoplasmic reticulum in frog muscle (Abstract). J. Physiol. London 175: 10P–11P, 1964.
 222. Page, S. G. A comparison of the fine structures of frog slow and twitch muscle fibres. J. Cell Biol. 26: 477–497, 1965.
 223. Page, S. G. Fine structure of tortoise skeletal muscle. J. Physiol. London 197: 709–715, 1968.
 224. Page, S. G. Structure and some contractile properties of fast and slow muscles of the chicken. J. Physiol. London 205: 131–145, 1969.
 225. Page, S. G., and R. Niedergerke. Structures of physiological interest in the frog heart ventricle. J. Cell Sci. 11: 179–203, 1972.
 226. Palade, P. T., and W. Almers. Slow Na and Ca currents across the membrane of frog striated muscle fibres (Abstract). Biophys. J. 21: 168a, 1978.
 227. Paolini, P. J., K. P. Roos, and R. J. Baskin. Light diffraction studies of sarcomere dynamics in single skeletal muscle fibers. Biophys. J. 20: 221–232, 1977.
 228. Papir, D. The effect of glycerol treatment on crab muscle fibres. J. Physiol. London 230: 313–330, 1973.
 229. Pasquali‐Ronchetti, I. The ultrastructural organization of femoral muscles in Musca domestica (Diptera). Tissue Cell 2: 339–354, 1970.
 230. Peachey, L. D. Morphological Pathways for Impulse Conduction in Muscle Cells. New York: Rockefeller Inst., 1959. PhD Thesis.
 231. Peachey, L. D. Structure and function of slow striated muscle. In: Biophysics of Physiological and Pharmacological Actions, edited by A. M. Shanes. Washington, DC: Am. Assoc. Adv. Sci., 1961, p. 391–411.
 232. Peachey, L. D. Structure of the longitudinal body muscles of amphioxus. J. Biophys. Biochem. Cytol. 10 (4), Suppl.: 159–176, 1961.
 233. Peachey, L. D. The sarcoplasmic reticulum and transverse tubules of the frog's sartorius. J. Cell Biol. 25 (3, pt. 2): 209–231, 1965.
 234. Peachey, L. D. Transverse tubules in excitation‐contraction coupling. Federation Proc. 24: 1124–1134, 1965.
 235. Peachey, L. D. Structure of the sarcoplasmic reticulum and T‐system of striated muscle. In: Proc. Int. Congr. Physiol. Sci., 23rd, Tokyo, 1965, vol. 4, p. 388–398.
 236. Peachey, L. D. Membrane systems in crab fibers. Am. Zool. 7: 505–513, 1967.
 237. Peachey, L. D. The structure of the extraocular muscle fibers of mammals. In: The Control of Eye Movements, edited by P. Bach‐y‐Rita, C. C. Collins, and J. E. Hyde. New York: Academic, 1971, p. 47–66.
 238. Peachey, L. D. Stereoscopic electron microscopy: principles and methods. Bull. Electron Microsc. Soc. Am. 8: 15–21, 1978.
 239. Peachey, L. D. Three‐dimensional structure of the T‐system of skeletal muscle cells. In: Proc. Int. Congr. Physiol. Sci., 28th, Budapest, 1980, vol. 14, p. 299–311.
 240. Peachey, L. D., and B. R. Eisenberg. Helicoids in the T system and striations of frog skeletal muscle fibers seen by high voltage electron microscopy. Biophys. J. 22: 145–154, 1978.
 241. Peachey, L. D., and C. Franzini‐Armstrong. Three‐dimensional visualization of the T‐system of frog muscle using high voltage electron microscopy and a lanthanum stain. Annu. Proc. Electron Microsc. Soc. Am., 35th, Boston, 1977, p. 570–571.
 242. Peachey, L. D., and C. Franzini‐Armstrong. Observation of the T‐system of rat skeletal muscle fibers in three dimensions using high voltage electron microscopy and the Golgi stain (Abstract). Biophys. J. 21: 61a, 1978.
 243. Peachey, L. D., C. Hudson, and P. Bach‐Y‐Rita. Marking extraocular muscle fibers for physiological‐morphological correlation (Abstract). Proc. Int. Congr. Physiol. Sci., 25th, Munich, 1971, vol. 9, p. 443.
 244. Peachey, L. D., and A. F. Huxley. Local activation and structure of slow striated muscle fibers of the frog (Abstract). Federation Proc. 19: 257, 1960.
 245. Peachey, L. D., and A. F. Huxley. Structural identification of twitch and slow striated muscle fibers of the frog. J. Cell Biol. 13: 177–180, 1962.
 246. Peachey, L. D., and A. F. Huxley. Transverse tubules in crab muscle (Abstract). J. Cell Biol. 23: 70a–71a, 1964.
 247. Peachey, L. D., and K. R. Porter. Intracellular impulse conduction in muscle cells. Science 129: 721–722, 1959.
 248. Peachey, L. D., and R. F. Schild. The distribution of the T‐system along the sarcomeres of frog and toad sartorius muscles. J. Physiol. London 194: 249–258, 1968.
 249. Peachey, L. D., M. Takeichi, and A. C. Nag. Muscle fiber types and innervation in adult cat extraocular muscles. In: Exploratory Concepts in Muscular Dystrophy II. Amsterdam: Excerpta Med., 1974, p. 246–254.
 250. Peachey, L. D., R. A. Waugh, and J. R. Sommer. High voltage electron microscopy of sarcoplasmic reticulum (Abstract). J. Cell Biol. 63: 262a, 1974.
 251. Pellegrino, C., and C. Franzini. An electron microscope study of denervation atrophy in red and white skeletal muscle fibers. J. Cell Biol. 17: 327–349, 1963.
 252. Pette, D. (editor). Plasticity of Muscle. Berlin: Gruyter, 1980.
 253. Pilar, G. Further study of the electrical and mechanical responses of slow fibers in cat extraocular muscles. J. Gen. Physiol. 50: 2289–2300, 1967.
 254. Popescu, L. M., and I. Diculescu. Calcium in smooth muscle sarcoplasmic reticulum in situ. Conventional and X‐ray analytical electron microscopy. J. Cell Biol. 67: 911–918, 1975.
 255. Porter, K. R., and G. E. Palade. Studies on the endoplasmic reticulum. III. Its form and distribution in striated muscle cells. J. Biophys. Biochem. Cytol. 3: 269–300, 1957.
 256. Potter, J. D., J. D. Johnson, and F. Mandel. Fluorescence stopped flow measurements of Ca2+ and Mg2+ binding to parvalbumin (Abstract). Federation Proc. 37: 1608, 1978.
 257. Pringle, J. Arthropod muscle. In: The Structure and Function of Muscle (2nd ed.), edited by G. H. Bourne. New York: Academic, 1972, vol. 1, p. 491–562.
 258. Pringle, J. W. S. The muscles and sense organs involved in insect flight. In: Insect Flight, edited by R. C. Rainey. Oxford, UK: Blackwell, 1976, p. 3–15. (Symp. R. Entomol. Soc. London, 7th.)
 259. Rayns, D. G., C. E. Devine, and C. L. Sutherland. Freeze‐fracture studies of membrane systems in vertebrate muscle. I. Striated muscle. J. Ultrastruct. Res. 50: 306–321, 1975.
 260. Reger, J. F. The fine structure of neuromuscular junctions and the sarcoplasmic reticulum of extrinsic eye muscles of Fundulus heteroclitus. J. Biophys. Biochem. Cytol. 10 (4), Suppl.: 111–121, 1961.
 261. Reger, J. F. A comparative study on striated muscle fiber of the antenna and the claw muscle of the crab Primixie sp. J. Ultrastruct. Res. 20: 72–82, 1967.
 262. Retzius, G. Muskelfibrille und Sarcoplasma. Biol. Unters. Neue Folge 1: 51–88, 1890.
 263. Reuben, J. P., D. P. Purpura, M. V. L. Bennett and E. R. Kandel (editors). Electrobiology of Nerve, Muscle and Synapse. New York: Raven, 1976.
 264. Revel, J. P. The sarcoplasmic reticulum of the bat cricothyroid muscle. J. Cell Biol. 12: 571–588, 1962.
 265. Revel, J. P., and M. Karnovsky. Hexagonal array of subunits in intercellular junctions of the mouse heart and liver. J. Cell Biol. 33: C7–C12, 1967.
 266. Rogus, E., and K. L. Zierler. Sodium and water contents of sarcoplasm and sarcoplasmic reticulum in rat skeletal muscle: effects of anisotonic media, ouabain and external sodium. J. Physiol. London 233: 227–270, 1973.
 267. Rollet, A. Über die Flossenmuskeln des Seepferdchens (Hippocampus antiquorum) und über Muskel Struktur in Allgemeinen. Arch. Mikrosk. Anat. 32: 233–266, 1888.
 268. Rosenbluth, J. Sarcoplasmic reticulum of an unusually fast‐acting crustacean muscle. J. Cell Biol. 42: 534–547, 1969.
 269. Rosenbluth, J. Oblique striated muscle. In: The Structure and Function of Muscle (2nd ed.), edited by G. H. Bourne. New York: Academic, 1972, vol. 1, p. 389–420.
 270. Rowland, L. P. (editor). Pathogenesis of Human Muscular Dystrophies. Amsterdam: Excerpta Med., 1976. (Int. Congr. Ser. 404.)
 271. Rubio, R., and N. Sperelakis. Penetration of horseradish peroxidase into the terminal cisternae of frog skeletal muscle fibers and blockade of caffeine contracture by Ca++ depletion. Z. Zeilforsch. Mikrosk. Anat. 124: 57–71, 1972.
 272. RÜDel, R., and F. Zite‐Ferenczy. Interpretation of light diffraction by cross‐striated muscle as Bragg reflection of light by the lattice of contractile proteins. J. Physiol. London 290: 317–330, 1979.
 273. Rudel, R., and F. Zite‐Ferenczy. Efficiency of light diffraction by cross‐striated muscle fibers under stretch and during isometric contraction. Biophys. J. 30: 507–516, 1980.
 274. Sanchez, J. A., and E. Stefani. Inward calcium current in twitch muscle fibres of the frog. J. Physiol. London 283: 197–209, 1978.
 275. Sandow, A. Excitation‐contraction coupling in muscular response. Yale J. Biol. Med. 25: 176–201, 1952.
 276. Sandow, A. Excitation‐contraction coupling in skeletal muscle. Pharmacol. Rev. 17: 265–320, 1965.
 277. Sanes, J. R. Laminin, fibronectin, and collagen in synaptic and extrasynaptic portions of muscle fiber basement membrane. J. Cell Biol. 93: 442–451, 1982.
 278. Sanger, J. W. Sarcoplasmic reticulum in the cross striated adductor muscle of the bay scallop Aquipecten iridians. Z. Zeilforsch. Mikrosk. Anat. 118: 156–161, 1971.
 279. Sawada, H., H. Ishikawa, and E. Yamada. High resolution scanning electron microscopy of frog sartorius muscle. Tissue Cell 10: 179–190, 1978.
 280. Scales, D. J., and T. Yasumura. Stereoscopic views of a dystrophic sarcotubular system: selective enhancement by a modified Golgi stain. J. Ultrastruct. Res. 78: 193–205, 1982.
 281. Schiaffino, S., and A. Margreth. Coordinated development of the sarcoplasmic reticulum and T system during postnatal differentiation of rat skeletal muscle. J. Cell Biol. 41: 855–875, 1969.
 282. Schmalbruch, H. Regeneration of soleus muscles of rat autografted in toto as studied by electron microscopy. Cell Tissue Res. 177: 159–180, 1977.
 283. Schneider, M. F. Membrane charge movement and depolarization‐contraction coupling. Annu. Rev. Physiol. 48: 507–517, 1981.
 284. Schneider, M. F., and W. K. Chandler. Voltage dependent charge movement in skeletal muscle: a possible step in excitation‐contraction coupling. Nature London 242: 244–246, 1973.
 285. Schotland, D. L. An electron microscopic investigation of myotonic dystrophy. J. Neuropathol. Exp. Neurol. 29: 241–253, 1970.
 286. Schultz, E., A. W. Clark, A. Suzuki, and R. G. Cassens. Rattlesnake shaker muscle. II. Fine structure. Tissue Cell 12: 335–351, 1980.
 287. Selverston, A. Structure and function of the transverse tubular system in crustacean muscle. Am. Zool. 7: 515–525, 1967.
 288. Sherman, R. G., and A. R. Luff. Structural features of the tarsal claw muscles of the spider Euripelma marxi Simon. Can. J. Zool. 49: 1549–1556, 1971.
 289. Shuman, H., A. V. Somlyo, and A. P. Somlyo. Quantitative electron probe microanalysis of biological thin sections: methods and validity. Ultramicroscopy 1: 317–339, 1976.
 290. Simpson, F. O., and S. J. Oertelis. Relationship of the sarcoplasmic reticulum to sarcolemma in sheep cardiac muscle. Nature London 189: 758–759, 1961.
 291. Skoglund, C. R. Functional analysis of swim‐bladder muscles engaged in sound production of the toadfish. J. Biophys. Biochem. Cytol. 10 (4), Suppl.: 187–200, 1961.
 292. Smith, D. S. Reticular organization within the striated muscle cell. An historical survey of light microscopic studies. J. Biophys. Biochem. Cytol. 10 (4), Suppl.: 61–87, 1961.
 293. Smith, D. S. The structure of insect fibrillar flight muscle. A study made with special reference to the membrane systems of the fiber. J. Biophys. Biochem. Cytol. 10: 123–158, 1961.
 294. Smith, D. S. The organization of flight muscle fibers in the odonata. J. Cell Biol. 28: 109–126, 1966.
 295. Smith, D. S., and H. C. Aldrich. Membrane systems of freeze‐etched striated muscle. Tissue Cell 3: 261–281, 1971.
 296. Smith, D. S., R. J. Baerwald, and M. A. Hart. The distribution of orthogonal assemblies and other intercalated particles in frog sartorius and rabbit sacrospinalis muscle. Tissue Cell 7: 369–382, 1975.
 297. Somlyo, A. P., A. V. Somlyo, and H. Shuman. Electron probe analysis of vascular smooth muscle: composition of mitochondria, nuclei, and cytoplasm. J. Cell Biol. 81: 316–335, 1979.
 298. Somlyo, A. V. Bridging structures spanning the junctional gap at the triad of skeletal muscle. J. Cell Biol. 80: 743–750, 1979.
 299. Somlyo, A. V., H. Gonzalez‐Serratos, H. Shuman, G. Mcclellan, and A. P. Somlyo. Calcium release and ionic changes in the sarcoplasmic reticulum of tetanized muscle: an electron‐probe study. J. Cell Biol. 90: 577–594, 1981.
 300. Somlyo, A. V., H. Shuman, and A. P. Somlyo. Elemental distribution in striated muscle and the effects of hypertonicity. J. Cell Biol. 74: 828–857, 1977.
 301. Somlyo, A. V., and J. Silcox. Cryoultramicrotomy for electron probe analysis. In: Microbeam Analysis in Biology, edited by C. Lechene and R. Warner. New York: Academic, 1979, p. 535–555.
 302. Sommer, J. R., P. C. Dolber, and I. Taylor. Filipin‐cholesterol complexes in the sarcoplasmic reticulum of frog skeletal muscle. J. Ultrastruct. Res. 72: 272–285, 1980.
 303. Sommer, J. R., and E. A. Johnson. Cardiac muscle. A comparative study of Purkinje fibers and ventricular fibers. J. Cell Biol. 36: 497–526, 1968.
 304. Sommer, J. R., and E. A. Johnson. Ultrastructure of cardiac muscle. In: Handbook of Physiology. The Cardiovascular System, edited by R. M. Berne and N. Sperelakis. Bethesda, MD: Am. Physiol. Soc., 1979, sect. 2, vol. I, chapt. 5, p. 113–186.
 305. Sommer, J. R., R. L. Steere, E. A. Johnson, and P. H. Jewett. Ultrastructure of cardiac muscle. A comparative review with emphasis on the muscle fibers of the ventricles. In: Hibernation and Hypothermia: Perspectives and Challenges, edited by F. E. South, J. P. Hannon, J. R. Willis, E. T. Pengelley, and N. R. Alport. Amsterdam: Elsevier, 1972, p. 255–291.
 306. Sommer, J. R., N. R. Wallace, and W. Hasselbach. The collapse of the sarcoplasmic reticulum in skeletal muscle. Z. Naturforsch. 33: 561–573, 1978.
 307. Sommer, J. R., N. R. Wallace, and J. Junker. The intermediate cisterna of the sarcoplasmic reticulum of skeletal muscle. J. Ultrastruct. Res. 71: 126–142, 1980.
 308. Sommer, J. R., and R. A. Waugh. The ultrastructure of the mammalian cardiac muscle cell with special emphasis on the tubular membrane systems. A review. Am. J. Pathol. 82: 192–221, 1976.
 309. Sommerkamp, H. Das Substrat der Dauerverkürzung am Froschmuskel. Arch. Exp. Pathol. Pharmakol. 128: 99–115, 1928.
 310. Stefani, E., and D. J. Chiarandini. Skeletal muscle: dependence of potassium contractures on extracellular calcium. Pfluegers Arch. Gesamte Physiol. Menschen Tiere 343: 143–150, 1973.
 311. Stephenson, E. W. Activation of fast skeletal muscle: contributions of studies on skinned fibers. Am. J. Physiol. 240 (Cell Physiol. 9): C1–C19, 1981.
 312. Stephenson, E. W., and R. J. Podolsky. Influence of magnesium on chloride‐induced calcium release in skinned muscle fibers. J. Gen. Physiol. 69: 17–35, 1977.
 313. Street, S. F., and R. W. Ramsay. Sarcolemma: transmitter of active tension in frog skeletal muscle. Science 149: 1379–1380, 1965.
 314. Tameyasu, T., N. Ishide, and G. H. Pollack. Discrete sarcomere length distributions in skeletal muscle. Biophys. J. 37: 489–492, 1981.
 315. Tiegs, O. W. The flight muscles of insects—their anatomy and histology; with some observations on the structure of striated muscle in general. Philos. Trans. R. Soc. London Ser. B 238: 221–348, 1955.
 316. Toda, M., T. Yamamoto, and Y. Tonomura. Molecular mechanism of active calcium transport by sarcoplasmic reticulum. Physiol. Rev. 58: 1–79, 1978.
 317. Tormey, J. M. Differences in membrane configuration between osmium tetroxide‐fixed and glutaraldehyde‐fixed ciliary epithelium. J. Cell Biol. 23: 658–664, 1964.
 318. Veratti, E. Ricerche sulla fine struttura della fibra muscolare striata. Mem. 1st. Lombardo Cl. Sci. Mat. Nat. 19: 87–133, 1902.
 319. Veratti, E. Investigations on the fine structure of the striated muscle fiber. J. Biophys. Biochem. Cytol. 10 (4), Suppl.: 3–59, 1961. (Paper from 1902, transl, by C. Bruni, H. S. Bennett, F. deKoven, and D. deKoven.)
 320. Walker, S. M., and M. B. Edge. The sarcoplasmic reticulum and development of Z lines in skeletal muscle fibers of fetal and postnatal rats. Anat. Rec. 169: 661–677, 1971.
 321. Walker, S. M., and G. R. Schrodt. Continuity of the T system with the sarcolemma in rat skeletal muscle fibers. J. Cell Biol. 27: 671–677, 1965.
 322. Walker, S. M., and G. R. Schrodt. Triads in skeletal muscle fibers of 19‐day fetal rats. J. Cell Biol. 37: 564–569, 1968.
 323. Walker, S. M., G. R. Schrodt, and M. Bingham. Evidence for connections of the sarcoplasmic reticulum with the sarcolemma and with the Z line in skeletal muscle fibers of fetal and newborn rats. Am. J. Phys. Med. 48: 63–77, 1969.
 324. Waugh, R. A., J. R. Sommer, and L. D. Peachey. Cardiac sarcoplasmic reticulum: distribution and ultrastructure revealed by selective staining. Circulation 50: 111–13, 1974.
 325. Waugh, R. A., T. L. Spray, and J. R. Sommer. Fenestrations of sarcoplasmic reticulum. Delineation by lanthanum acting as a fortuitous tracer and in situ negative stain. J. Cell Biol. 59: 254–260, 1973.
 326. Weber, A. M., R. Herz, and I. Reiss. Study of the kinetics of calcium transport by isolated fragmented sarcoplasmic reticulum. Biochem. J. 345: 329–369, 1966.
 327. Winegrad, S. Intracellular calcium movements of frog skeletal muscle during recovery from tetanus. J. Gen Physiol. 51: 65–83, 1968.
 328. Winegrad, S. The intracellular site of calcium activation of contraction in frog skeletal muscle. J. Gen. Physiol. 55: 77–88, 1970.
 329. Yeh, Y., R. J. Baskin, R. L. Lieber, and K. P. Roos. Theory of light diffraction by single skeletal muscle fibers. Biophys. J. 29: 509–522, 1980.
 330. Zampighi, E. G., J. Vergara, and F. Ramon. The connection between the T‐tubules and the plasma membrane in frog skeletal muscle J. Cell Biol. 64: 734–740, 1975.

Contact Editor

Submit a note to the editor about this article by filling in the form below.

* Required Field

How to Cite

Lee D. Peachey, Clara Franzini‐Armstrong. Structure and Function of Membrane Systems of Skeletal Muscle Cells. Compr Physiol 2011, Supplement 27: Handbook of Physiology, Skeletal Muscle: 23-71. First published in print 1983. doi: 10.1002/cphy.cp100102