Comprehensive Physiology Wiley Online Library

Energetics of Muscle Contraction

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Historical Perspectives
1.1 Nature of the Muscle Machine
1.2 Chemical Discoveries
1.3 Energetics as an Analytical Tool
1.4 Direct Measurements of Chemical Change
1.5 Summary
2 Chemical Reactions and Metabolic Principles
2.1 Adenosine Triphosphatases
2.2 Creatine Phosphokinase
2.3 Adenylate Kinase
2.4 Adenylate Deaminase and the Purine Nucleotide Cycle
2.5 Glycogenolysis and Glycolysis
2.6 Oxidative Metabolism
3 Basic Energetic Model
4 Thermodynamics
5 Energy Balance
5.1 Myothermic Method
5.2 Biochemical Method
6 Results of Energy Balance Experiments
6.1 Energy Balance Studies in Rana temporaria
6.2 Energy Balance Studies in Rana pipiens
6.3 Amphibian Muscles
6.4 Mammalian Muscles
7 Energetics of Muscles that Shorten or are Stretched
8 New Directions
8.1 Phosphorus Nuclear Magnetic Resonance Spectroscopy
8.2 Use of Single Fibers
Figure 1. Figure 1.

Time course of heat production during a maintained isometric tetanus of frog muscle at various temperatures. [Redrawn from Hartree and Hill .]

Figure 2. Figure 2.

Variations of external mechanical work and heat in excess of isometric heat as a function of load in isotonic afterloaded contractions; 1 J = 107 ergs. [From Fenn .]

Figure 3. Figure 3.

Measurements of total energy output or chemical change as a function of load in working contractions studied by different investigators. All values are relative to a reference isometric contraction (+). ▴, ▪, □, Experiments made above 10°C; •, ×, Δ, experiments made near 0°C. Interrupted line depicts expected energy output as the sum of activation heat, shortening heat, and external work done.

From Woledge , © 1971, with permission from Pergamon Press, Ltd
Figure 4. Figure 4.

Energy output in single isotonic twitches of frog sartorius muscles as a function of load. Filled circle, heat output in an isometric twitch; curve w, represents external work done; curve h + w, total energy released; line h vs. load, isometric twitch heat measured at increasingly long lengths and therefore at decreasing isometric forces; line hw is the difference between uppermost and lowermost curve.

Adapted from Homsher et al.
Figure 5. Figure 5.

Model of behavior of energy‐rich phosphate compounds' as a function of extent of PCr splitting, ξ ∼ P, for coupled equilibria of creatine Phosphokinase and adenylate kinase reactions. Conditions for resting muscle are plotted at the origin.

Adapted from Vincent and Blair
Figure 6. Figure 6.

A: activation of glycogen Phosphorylase during contractile activity of aerobic frog muscle. B: fractional Phosphorylase activity as a function of the extent of high‐energy phosphate splitting (ξ ∼ P) during a single isometric tetanus. [A from Mommaerts et al. ; B data from M. J. Kushmerick, unpublished observations.]

Figure 7. Figure 7.

Scheme of steps in mitochondrial oxidative phosphorylation omitting mechanisms of generating proton gradients. Each site is a mechanism for formation of one ATP from ADP and Pi coupled to the proton motive force generated by the stepwise oxidation of one reducing equivalent by one‐half O2. Some substrates enter the chain distal to site 1 and bypass first ATP‐generating site.

Figure 8. Figure 8.

Fluorescent signals obtained from intact anuran muscles. A: record of a decrease in fluorescence after a twitch at 12°C, which indicates a transient decrease (or oxidation) of NADH. B: records of fluorescence changes after a 0.5‐s tetanus at 20°C showing a transient increase in fluorescence or increase in NADH, which in A is partly obscured by a movement artifact. In B this artifact has been subtracted, and the fast transient increase in NADH is blocked by iodoacetate, which indicates that a portion of the response can be attributed to glycolytic redox transients in the cytosol. [A from Jöbsis and Duffield ; B from Godfraind‐de Becker .]

Figure 9. Figure 9.

Oxygen consumption as a function of time in a mitochondrial suspension (A) and in intact frog sartorius muscle at 0°C (B). After addition of ADP to a mitochondrial suspension, respiration rate becomes maximal, characteristic of state 3, and returns to state 4 when added ADP is completely phosphorylated. The first addition of ADP is about twice the amount of the second. Two recovery O2 consumption records are presented in B, one from each member of a pair of sartorius muscles from 1 animal. There is a diffusional delay between tetanus and first sign of increased O2 consumption. Rate of O2 consumption after a single contraction is always much less (here about Va) than the maximal respiratory capability of the muscle . [B from Paul and Kushmerick .]

Figure 10. Figure 10.

Chemical changes during contraction and subsequent recovery during which initial steady‐state conditions are restored.

Figure 11. Figure 11.

Relationship between total enthalpy production (h + w) and explained enthalpy during isometric tetanuses of various durations. A and B: explained enthalpy (○) and h + w (•). C: a scheme in which it is imagined that the unknown reaction goes to completion and is added linearly to the stable rate of enthalpy production to give observed total enthalpy production. [A from Homsher et al. ; B from Curtin and Woledge .]

Figure 12. Figure 12.

Utilization of chemical energy during contraction as a function of tension‐time integral for isometric tetanuses up to 20 s in duration. A: initial chemical changes (initial ξ ∼ P); B: recovery O2 consumption (recovery ξ ∼ P). Sartorii from Rana temporaria were studied at O°C. In A and B ξ ∼ P and ξo2 are plotted separately. C: ξ ∼ P is replotted (•); ξo2 × 6.3 is plotted on the same graph (▪). Break in upper curve in C occurs between 5 and 10 s of stimulation. Tension‐time integral for each second of stimulation is approximately 2.1 kg · cm‐1 · s−1 · g−1. (M. J. Kushmerick, unpublished observations.)

Figure 13. Figure 13.

Energy imbalance in Rana temporaria (left) and Rana pipiens (right). Open symbols and full line, h + w; closed symbols and dashed line, explained enthalpy. Dotted curve on right is the unexplained enthalpy. [From Homsher and Kean .

Reproduced, with permission, from Annu. Rev, Physiol., vol. 40, © 1978 by Annual Reviews, Inc
Figure 14. Figure 14.

Relationships between initial changes in high‐energy phosphate compounds [Δ ∼ P/g, (ξ ∼ P)] and stimulus duration (A) and tension‐time integral (B). Mean values ± SE are shown. Relationships between recovery O2 consumption [ΔO2/g, (ξo2)] and tetanus duration (C) and tension‐time integral (D) are shown for data obtained in 1 muscle. [From Kushmerick and Paul .]

Figure 15. Figure 15.

Initial and recovery chemical changes as a function of duration of isometric tetanus. •, Direct measurements of ξ ∼ P; ○, measurements of ξo2 multiplied by a factor of 4 to scale with ξ ∼ P. Regression equations given in insert. Aerobic sartorii of Rana pipiens at 0°C. [Data from Kushmerick and Paul .]

Figure 16. Figure 16.

Relationship between initial changes in high‐energy phosphates, ξ ∼ P (open symbols) and high‐energy phosphate resynthesis by recovery metabolism (closed symbols) as a function of tension‐time integral. Contraction durations were 0.5, 1, 3, and 5 s. Circles, aerobic muscles; squares, anaerobic muscles; filled circles, 6.3 × ξo2; filled squares, 1.5 × ξ lactate. Aerobic and anaerobic sartorii of Rana pipiens at 20°C. [Data replotted from DeFuria and Kushmerick .]

Figure 17. Figure 17.

Mechanical power, chemical power, and efficiency of muscular work as a function of velocity of shortening. Muscles were constrained to shorten at constant velocities. A: rate of mechanical work‐mechanical power. B: rate of utilization of high‐energy phosphates or chemical power input, measured directly as ATP splitting in fluorodinitrobenzene‐treated muscles (creatine Phosphokinase blocked). C: efficiency of work performance derived from the data in A and B (solid line). Interrupted line is efficiency after subtracting an estimated amount of ATP splitting thought to represent nonactomyosin energy costs. [From Kushmerick and Davies .]

Figure 18. Figure 18.

Calculations based on the cross‐bridge model of Eisenberg, Hill, and Chen . /o, rate of nigh‐energy phosphate splitting normalized to the isometric rate, η, Efficiency of chemomechani‐cal coupling; , number of ATP molecules hydrolyzed per unit distance shortened. All parameters graphed as a function of steady‐state velocity of shortening. [From Eisenberg et al. .]

Figure 19. Figure 19.

31P NMR spectra of cat biceps muscle . Muscle was perfused in vitro through branches of capillary artery with an oxygenated synthetic commercial fluorocarbon suspension (Fluosol‐43) containing papaverine at 30 μg/ml; flow was 0.2 ml/min for this 3‐g muscle. Upper curve is spectrum obtained with a single NMR scan; lower curve is spectrum obtained by averaging 40 scans, each taken at 15‐s intervals. Identification of the peaks from left to right: Pi; PCr; γ‐, α‐, and β‐phosphorus of ATP. Shoulder on α‐ATP is probably NAD/NADH.



Figure 1.

Time course of heat production during a maintained isometric tetanus of frog muscle at various temperatures. [Redrawn from Hartree and Hill .]



Figure 2.

Variations of external mechanical work and heat in excess of isometric heat as a function of load in isotonic afterloaded contractions; 1 J = 107 ergs. [From Fenn .]



Figure 3.

Measurements of total energy output or chemical change as a function of load in working contractions studied by different investigators. All values are relative to a reference isometric contraction (+). ▴, ▪, □, Experiments made above 10°C; •, ×, Δ, experiments made near 0°C. Interrupted line depicts expected energy output as the sum of activation heat, shortening heat, and external work done.

From Woledge , © 1971, with permission from Pergamon Press, Ltd


Figure 4.

Energy output in single isotonic twitches of frog sartorius muscles as a function of load. Filled circle, heat output in an isometric twitch; curve w, represents external work done; curve h + w, total energy released; line h vs. load, isometric twitch heat measured at increasingly long lengths and therefore at decreasing isometric forces; line hw is the difference between uppermost and lowermost curve.

Adapted from Homsher et al.


Figure 5.

Model of behavior of energy‐rich phosphate compounds' as a function of extent of PCr splitting, ξ ∼ P, for coupled equilibria of creatine Phosphokinase and adenylate kinase reactions. Conditions for resting muscle are plotted at the origin.

Adapted from Vincent and Blair


Figure 6.

A: activation of glycogen Phosphorylase during contractile activity of aerobic frog muscle. B: fractional Phosphorylase activity as a function of the extent of high‐energy phosphate splitting (ξ ∼ P) during a single isometric tetanus. [A from Mommaerts et al. ; B data from M. J. Kushmerick, unpublished observations.]



Figure 7.

Scheme of steps in mitochondrial oxidative phosphorylation omitting mechanisms of generating proton gradients. Each site is a mechanism for formation of one ATP from ADP and Pi coupled to the proton motive force generated by the stepwise oxidation of one reducing equivalent by one‐half O2. Some substrates enter the chain distal to site 1 and bypass first ATP‐generating site.



Figure 8.

Fluorescent signals obtained from intact anuran muscles. A: record of a decrease in fluorescence after a twitch at 12°C, which indicates a transient decrease (or oxidation) of NADH. B: records of fluorescence changes after a 0.5‐s tetanus at 20°C showing a transient increase in fluorescence or increase in NADH, which in A is partly obscured by a movement artifact. In B this artifact has been subtracted, and the fast transient increase in NADH is blocked by iodoacetate, which indicates that a portion of the response can be attributed to glycolytic redox transients in the cytosol. [A from Jöbsis and Duffield ; B from Godfraind‐de Becker .]



Figure 9.

Oxygen consumption as a function of time in a mitochondrial suspension (A) and in intact frog sartorius muscle at 0°C (B). After addition of ADP to a mitochondrial suspension, respiration rate becomes maximal, characteristic of state 3, and returns to state 4 when added ADP is completely phosphorylated. The first addition of ADP is about twice the amount of the second. Two recovery O2 consumption records are presented in B, one from each member of a pair of sartorius muscles from 1 animal. There is a diffusional delay between tetanus and first sign of increased O2 consumption. Rate of O2 consumption after a single contraction is always much less (here about Va) than the maximal respiratory capability of the muscle . [B from Paul and Kushmerick .]



Figure 10.

Chemical changes during contraction and subsequent recovery during which initial steady‐state conditions are restored.



Figure 11.

Relationship between total enthalpy production (h + w) and explained enthalpy during isometric tetanuses of various durations. A and B: explained enthalpy (○) and h + w (•). C: a scheme in which it is imagined that the unknown reaction goes to completion and is added linearly to the stable rate of enthalpy production to give observed total enthalpy production. [A from Homsher et al. ; B from Curtin and Woledge .]



Figure 12.

Utilization of chemical energy during contraction as a function of tension‐time integral for isometric tetanuses up to 20 s in duration. A: initial chemical changes (initial ξ ∼ P); B: recovery O2 consumption (recovery ξ ∼ P). Sartorii from Rana temporaria were studied at O°C. In A and B ξ ∼ P and ξo2 are plotted separately. C: ξ ∼ P is replotted (•); ξo2 × 6.3 is plotted on the same graph (▪). Break in upper curve in C occurs between 5 and 10 s of stimulation. Tension‐time integral for each second of stimulation is approximately 2.1 kg · cm‐1 · s−1 · g−1. (M. J. Kushmerick, unpublished observations.)



Figure 13.

Energy imbalance in Rana temporaria (left) and Rana pipiens (right). Open symbols and full line, h + w; closed symbols and dashed line, explained enthalpy. Dotted curve on right is the unexplained enthalpy. [From Homsher and Kean .

Reproduced, with permission, from Annu. Rev, Physiol., vol. 40, © 1978 by Annual Reviews, Inc


Figure 14.

Relationships between initial changes in high‐energy phosphate compounds [Δ ∼ P/g, (ξ ∼ P)] and stimulus duration (A) and tension‐time integral (B). Mean values ± SE are shown. Relationships between recovery O2 consumption [ΔO2/g, (ξo2)] and tetanus duration (C) and tension‐time integral (D) are shown for data obtained in 1 muscle. [From Kushmerick and Paul .]



Figure 15.

Initial and recovery chemical changes as a function of duration of isometric tetanus. •, Direct measurements of ξ ∼ P; ○, measurements of ξo2 multiplied by a factor of 4 to scale with ξ ∼ P. Regression equations given in insert. Aerobic sartorii of Rana pipiens at 0°C. [Data from Kushmerick and Paul .]



Figure 16.

Relationship between initial changes in high‐energy phosphates, ξ ∼ P (open symbols) and high‐energy phosphate resynthesis by recovery metabolism (closed symbols) as a function of tension‐time integral. Contraction durations were 0.5, 1, 3, and 5 s. Circles, aerobic muscles; squares, anaerobic muscles; filled circles, 6.3 × ξo2; filled squares, 1.5 × ξ lactate. Aerobic and anaerobic sartorii of Rana pipiens at 20°C. [Data replotted from DeFuria and Kushmerick .]



Figure 17.

Mechanical power, chemical power, and efficiency of muscular work as a function of velocity of shortening. Muscles were constrained to shorten at constant velocities. A: rate of mechanical work‐mechanical power. B: rate of utilization of high‐energy phosphates or chemical power input, measured directly as ATP splitting in fluorodinitrobenzene‐treated muscles (creatine Phosphokinase blocked). C: efficiency of work performance derived from the data in A and B (solid line). Interrupted line is efficiency after subtracting an estimated amount of ATP splitting thought to represent nonactomyosin energy costs. [From Kushmerick and Davies .]



Figure 18.

Calculations based on the cross‐bridge model of Eisenberg, Hill, and Chen . /o, rate of nigh‐energy phosphate splitting normalized to the isometric rate, η, Efficiency of chemomechani‐cal coupling; , number of ATP molecules hydrolyzed per unit distance shortened. All parameters graphed as a function of steady‐state velocity of shortening. [From Eisenberg et al. .]



Figure 19.

31P NMR spectra of cat biceps muscle . Muscle was perfused in vitro through branches of capillary artery with an oxygenated synthetic commercial fluorocarbon suspension (Fluosol‐43) containing papaverine at 30 μg/ml; flow was 0.2 ml/min for this 3‐g muscle. Upper curve is spectrum obtained with a single NMR scan; lower curve is spectrum obtained by averaging 40 scans, each taken at 15‐s intervals. Identification of the peaks from left to right: Pi; PCr; γ‐, α‐, and β‐phosphorus of ATP. Shoulder on α‐ATP is probably NAD/NADH.

References
 1. Abbott, B. C, and J. V. Howarth. Heat studies in excitable tissues. Physiol. Rev. 53: 120–158, 1973.
 2. Adrian, R. H., W. K. Chandler, and A. L. Hodgkin. The kinetics of mechanical activation in frog muscle. J. Physiol. London 204: 207–231, 1969.
 3. Aickin, C. C, and R. C. Thomas. Micro‐electrode measurement of the intracellular pH and buffering power of mouse soleus muscle fibres. J. Physiol. London 267: 791–810, 1977.
 4. Altschuld, R. A., and G. P. Brierley. Interaction between the creatine kinase of heat mitochondria and oxidative phosphorylation. J. Mol. Cell. Cardiol. 9: 875–893, 1977.
 5. Applegate, D. E., and E. Homsher. Calcium transport and ATPase activity in intact sarcoplasmic reticulum (Abstract). Federation Proc. 39: 294, 1980.
 6. Aubert, X. Le Couplage energetique de la contraction musculaire. Brussels: Arscia, 1956.
 7. Aubert, X., and G. Maréchal. La fraction labile de la thermogenese associée au maintien de la contraction isometrique. Arch. Int. Physiol. Biochim. 71: 282–283, 1963.
 8. BÁRÁNy, M. ATPase activity of myosin correlated with speed of muscle shortening. J. Gen. Physiol. 50: 197–216, 1967.
 9. Bessman, S. P., and A. Fonyo. The possible role of the mitochondrial bound creatine kinase in regulation of mitochondrial respiration. Biochem. Biophys. Res. Commun. 22: 597–602, 1966.
 10. Bessman, S. P., and P. J. Geiger. Transport of energy in muscle: the phosphorylcreatine shuttle. Science 211: 448–452, 1981.
 11. 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.
 12. Blix, M. Studien über Muskelwarme. Skand. Arch. Physiol. 12: 52–126, 1902.
 13. Blum, H. E., P. Lehky, L. Kohler, E. A. Stein, and E. H. Fischer. Comparative properties of vertebrate parvalbumin. J. Biol. Chem. 252: 2834–2838, 1977.
 14. Bowen, W. J., and T. D. Kerwin. The kinetics of myokinase. III. Studies of heat denaturation, the effects of salts and the state of equilibrium. Arch. Biochem. Biophys. 64: 278–284, 1956.
 15. Briggs, F. N., J. L. Poland, and R. J. Solaro. Relative capabilities of sarcoplasmic reticulum in fast and slow mammalian skeletal muscles. J. Physiol. London 266: 587–594, 1977.
 16. Brostrom, C. O., F. L. Hunkeler, and E. G. Krebs. The regulation of skeletal muscle Phosphorylase kinase by Ca++. J. Biol. Chem. 246: 1961–1967, 1971.
 17. Burt, C. T., T. Glonek, and M. BÁRÁNy. Analysis of phosphate metabolites, the intracellular pH and the state of adenosine triphosphate in intact muscle by phosphorus nuclear magnetic resonance. J. Biol. Chem. 251: 2584–2591, 1976.
 18. Cain, D. F., and R. E. Davies. Breakdown of adenosine triphosphate during a single contraction of working muscle. Biochem. Biophys. Res. Commun. 8: 361–366, 1962.
 19. Canfield, P., J. Lebacq, and G. Maréchal. Energy balance in frog sartorius muscle during an isometric tetanus at 20°C. J. Physiol. London 232: 467–483, 1973.
 20. Canfield, P., and G. Maréchal. Equilibrium of nucleotides in frog sartorius muscle during an isometric tetanus at 20°C. J. Physiol. London 232: 453–466, 1973.
 21. Carlson, F. D., D. J. Hardy, and D. R. Wilkie. Total energy production and phosphocreatine hydrolysis in the isotonic twitch. J. Gen. Physiol. 46: 851–882, 1963.
 22. Carlson, F. D., D. Hardy, and D. R. Wilkie. The relation between heat produced and phosphorylcreatine split during isometric contraction of frog's muscle. J. Physiol. London 189: 209–235, 1967.
 23. Carlson, F. D., and A. Siger. The mechanochemistry of muscular contraction. I. The isometric twitch. J. Gen. Physiol. 44: 33–60, 1960.
 24. Chance, B. Reaction of oxygen with the respiratory chain in cells and tissues. J. Gen. Physiol. 49, Suppl.: 163–188, 1965.
 25. Chance, B., and C. R. Williams. The respiratory chain and oxidative phosphorylation. Adv. Enzymol. Relat. Areas Mol. Biol. 17: 65–134, 1956.
 26. Chapell, J. B. Systems used for the transport of substrates into mitochondria. Br. Med. Bull. 24: 150–157, 1968.
 27. Collins, R. C, J. B. Posner, and F. Plum. Cerebral energy metabolism during electroshock seizures in mice. Am. J. Physiol. 218: 943–950, 1970.
 28. Crank, J. The Mathematics of Diffusion. London: Oxford Univ. Press, 1956.
 29. Crompton, M., M. Capano, and E. Carafoli. Respiration‐dependent efflux of magnesium ions from heart mitochondria. Biochem. J. 154: 735–742, 1976.
 30. Crow, M. T., and M. J. Kushmerick. The relationship between initial chemical change and recovery chemical input in isolated hindlimb muscles of the mouse. J. Gen. Physiol. 79: 147–166, 1982.
 31. Curtin, N. A., and R. E. Davies. Chemical and mechanical changes during stretching of activated frog skeletal muscle. Cold Spring Harbor Symp. Quant. Biol. 37: 619–626, 1973.
 32. Curtin, N. A., and R. E. Davies. Very high tension with very little ATP breakdown by active skeletal muscle. J. Mechanochem. Cell Motil. 3: 147–154, 1975.
 33. Curtin, N. A., C Gdlbert, D. M. Kretzschmar, and D. R. Wilkie. The effect of the performance of work on total energy output and metabolism during muscular contraction. J. Physiol. London 238: 455–472, 1974.
 34. Curtin, N. A., and R. C Woledge. Energetics of relaxation in frog muscle. J. Physiol. London 238: 437–446, 1974.
 35. Curtin, N. A., and R. C. Woledge. Energy balance in DNFB‐treated and untreated frog muscle. J. Physiol. London 246: 737–752, 1975.
 36. Curtin, N. A., and R. C. Woledge. A comparison of the energy balance in two successive isometric tetani of frog muscle. J. Physiol. London 270: 455–471, 1977.
 37. Curtin, N. A., and R. C Woledge. Energy changes and muscular contraction. Physiol. Rev. 58: 690–761, 1978.
 38. Curtin, N. A., and R. C Woledge. Chemical change and energy production during contraction of frog muscle: how are their time courses related? J. Physiol. London 288: 353–366, 1979.
 39. Curtin, N. A., and R. C Woledge. Chemical change, production of tension and energy following stretch of active muscle of frog. J. Physiol. London 297: 539–550, 1979.
 40. Danforth, W. H., E. Helmreich, and C. F. Cori. The effect of contraction and of epinephrine on the Phosphorylase activity of frog sartorius muscle. Proc. Natl. Acad. Sci. USA 48: 1191–1199, 1962.
 41. Davies, R. E. Molecular theory of muscle contraction: calcium‐dependent contractions with hydrogen bond formation plus ATP‐dependent extensions of part of the myosin‐actin cross‐bridges. Nature London 199: 1068–1074, 1963.
 42. Davies, R. E., D. Cain, and A. M. Delluva. The energy supply for muscular contraction. Ann. NY Acad. Sci. 81: 468–476, 1959.
 43. Dawson, M. J., D. G. Gadian, and D. R. Wilkie. Contraction and recovery of living muscles studied by 31P nuclear magnetic resonance. J. Physiol. London 267: 703–735, 1977.
 44. Dawson, M. J., D. G. Gadian, and D. R. Wilkie. Mechanical relaxation rate and metabolism studied in fatiguing muscle by phosphorus nuclear magnetic resonance. J. Physiol. London 299: 465–485, 1980.
 45. Dawson, J., D. Gower, K. M. Kretzschmar, and D. R. Wilkie. Heat production and chemical change in frog sartorius: a comparison R. pipiens with R. temporaria. J. Physiol. London 254: 41P–42P, 1975.
 46. Defuria, R. R., and M. J. Kushmerick. ATP utilization associated with recovery metabolism in anaerobic frog muscle. Am. J. Physiol. 232 (Cell Physiol. 1): C30–C36, 1977.
 47. Deweer, P., and A. G. Lowe. Myokinase equilibrium. J. Biol. Chem. 248: 2829–2835, 1973.
 48. Dixon, M., and E. C. Webb. Enzymes. New York: Academic, 1964, p. 274–275.
 49. Ebashi, S. E., and M. Endo. Calcium ion and muscle contraction. Prog. Biophys. Mol. Biol. 18: 123–183, 1968.
 50. Edman, K. A. P., G. Elzinga, and M. I. M. Noble. Enhancement of mechanical performance by stretch during tetanic contractions of vertebrate skeletal muscle fibres. J. Physiol. London 281: 139–155, 1978.
 51. Eggleston, L. V., and R. Hems. Separation of adenosine phosphates by paper chromatography and the equilibrium constant of the myokinase system. Biochem. J. 52: 156–160, 1952.
 52. Eggleton, G. P., and P. Eggleton. A method of estimating Phosphagen and some other phosphorus compounds in muscle tissue. J. Physiol. London 68: 193, 1929‐30.
 53. Eggleton, P., and G. P. Eggleton. The inorganic phosphate and a labile form of organic phosphate in the gastrocnemius of the frog. Biochem. J. 21: 190–195, 1927.
 54. Eisenberg, E., and L. E. Greene. The relation of muscle biochemistry to muscle physiology. Annu. Rev. Physiol. 42: 293–309, 1980.
 55. Eisenberg, E., T. Hill, and Y. Chen. Cross‐bridge model of muscle contraction. Biophys. J. 29: 195–226, 1980.
 56. Endo, M. Calcium release from the sarcoplasmic reticulum. Physiol. Rev. 57: 71–108, 1977.
 57. Engelhardt, V. A., and M. N. Lyubimova. Myosin and adenosinetriphosphatase. Nature London 144: 668, 1939.
 58. Erecińska, M., R. L. Veech, and D. F. Wilson. Thermodynamic relationships between the oxidation‐reduction reactions and the ATP synthesis in suspensions of isolated pigeon heart mitochondria. Arch. Biochem. Biophys. 160: 412–421, 1974.
 59. Erecińska, M., D. F. Wilson, and K. Nishiki. Homeostatic regulation of cellular energy metabolism: experimental characterization in vivo and fit to a model. Am. J. Physiol. 234 (Cell Physiol. 3): C82–C89, 1978.
 60. Feng, T. P. The heat tension ratio in prolonged tetanic contractions. Proc. R. Soc. London Ser. B 108: 522–537, 1931.
 61. Feng, T. P. The effect of length on the resting metabolism of muscle. J. Physiol. London 74: 441–454, 1932.
 62. Fenn, W. O. A quantitative comparison between the energy liberated and the work performed by the isolated sartorius muscle of the frog. J. Physiol. London 58: 175–203, 1923.
 63. Fenn, W. O. The relation between the work performed and the energy liberated in muscular contraction. J. Physiol. London 58: 373–395, 1924.
 64. Ferenczi, M. A., E. Homsher, R. M. Simmons, and D. R. Trentham. Reaction mechanism of the magnesium ion‐dependent adenosine triphosphatase of frog muscle myosin and subfragment 1. Biochem. J. 171: 165–175, 1978.
 65. Fick, A. Einige Bemerkungen zu Englemann's Abhandlung über den Ursprung der Muskelkraft. Pfluegers Arch. Gesamte Physiol. Menschen Tiere 53: 606–615, 1893.
 66. Fiske, C. H., and Y. Subbarow. The nature of inorganic phosphate in voluntary muscle. Science 65: 401–403, 1927.
 67. Fiske, C. H., and Y. Subbarow. The isolation and function of phosphocreatine. Science 67: 169–170, 1928.
 68. Fletcher, W. M., and F. G. Hopkins. Lactic acid in amphibian muscle. J. Physiol. London 35: 247–309, 1907.
 69. Fletcher, W. M., and F. G. Hopkins. The respiratory process in muscle and the nature of muscular motion. Proc. R. Soc. London Ser. B 89: 444–467, 1917.
 70. Folkow, B., and H. D. Halicka. A comparison between “red” and “white” muscle with respect to blood supply, capillary surface area and oxygen uptake during rest and exercise. Microvasc. Res. 1: 1–14, 1968.
 71. Ford, L. E., and R. J. Podolsky. Calcium uptake and force development by skinned muscle fibres in EGT A buffered solutions. J. Physiol. London 223: 1–19, 1972.
 72. Foster, D. O., and M. L. Frydman. Tissue distribution of cold‐induced thermogenesis in conscious warm‐ or cold‐acclimated rats re‐evaluated from changes in tissue blood flow: the dominant role of brown adipose tissue in the replacement of shivering by nonshivering thermogenesis. Can. J. Physiol. Pharmacol. 57: 257–270, 1979.
 73. Francis, S. H., B. P. Meriwether, and J. H. Park. Effects of photooxidation of Histidine‐38 on the various catalytic activities of glyceraldehyde‐3‐phosphate dehydrogenase. Biochemistry 12: 346–355, 1973.
 74. Frazer, A., and F. D. Carlson. Initial heat production in isometric frog muscles at 15°C. J. Gen. Physiol. 62: 271–285, 1973.
 75. Fry, D. M., and M. F. Morales. A reexamination of the effects of creatine on muscle protein synthesis in tissue culture. J. Cell Biol. 84: 204–297, 1980.
 76. Gadian, D. G., G. K. Radda, T. R. Brown, E. M. Chance, M. J. Dawson, and D. R. Wilkie. The activity of creatine kinase in frog skeletal muscle studied by saturation‐transfer nuclear magnetic resonance. Biochem. J. 195: 1–14, 1981.
 77. George, P., and R. J. Rutman. The “high energy phosphate bond” concept. Prog. Biophys. Biophys. Chem. 10: 2–53, 1960.
 78. Gilbert, C, K. M. Kretzschmar, D. R. Wilkie, and R. C. Woledge. Chemical change and energy output during muscular contraction. J. Physiol. London 218: 163–193, 1971.
 79. Godfraind‐De Becker, A. Heat production and fluorescence changes of toad sartorius muscle during aerobic recovery after a short tetanus. J. Physiol. London 223: 719–734, 1972.
 80. Gordon, A. M., A. F. Huxley, and F. J. Julian. The variation in isometric tension with sarcomere length in vertebrate muscle fibres. J. Physiol. London 184: 170–192, 1966.
 81. Gower, D., and K. M. Kretzschmar. Heat production and chemical change during isometric contraction of rat soleus muscle. J. Physiol. London 258: 659–671, 1976.
 82. Gupta, R. K., and R. D. Moore. 31P NMR studies of intracellular free Mg++ in intact frog skeletal muscle. J. Biol. Chem. 255: 3987–3992, 1980.
 83. Hansford, R. G. Control of mitochondrial substrate oxidation. Curr. Top. in Bioenerg. 10: 217–278, 1980.
 84. Harris, E. J. The stoichiometry of sodium ion movement from frog muscle. J. Physiol London 193: 455–458, 1967.
 85. Harris, S. I., R. S. Balaban, and L. J. Mandel. Oxygen consumption and cellular ion transport: evidence for adenosine triphosphate to O2 ratio near 6 in intact cell. Science 208: 1148–1150, 1980.
 86. Harting, J., and S. F. Velick. Acetyl phosphate formation catalyzed by glyceraldehyde‐3‐phosphate dehydrogenase. J. Biol. Chem. 207: 857–865, 1954.
 87. Hartree, W., and A. V. Hill. The regulation of the supply of energy in muscular contraction. J. Physiol. London 55: 133–158, 1921.
 88. Hassinen, I. C. Respiratory control in isolated perfused rat heart: role of the equilibrium relations between the mitochondrial electron carriers and the adenylate system. Biochim. Biophys. Acta 408: 319–330, 1975.
 89. Heilbrunn, L. V., and F. J. Wiercinski. The action of various cations on muscle protoplasm. J. Cell. Comp. Physiol. 29: 15–32, 1947.
 90. Heilmeyer, L. M. G., F. Meyer, R. H. Haschke, and E. H. Fischer. Control of Phosphorylase activity in a muscle glycogen particle II. Activation by calcium. J. Biol. Chem. 245: 6649–6656, 1970.
 91. Hellam, D. C, and R. J. Podolsky. Force measurements in skinned muscle fibres. J. Physiol. London 200: 807–819, 1969.
 92. Hill, A. V. The absolute mechanical efficiency of the contraction of an isolated muscle. J. Physiol. London 46: 435–469, 1913.
 93. Hill, A. V. The heat of shortening and the dynamic constants of muscle. Proc. R. Soc. London Ser. B 126: 136–195, 1938.
 94. Hill, A. V. Adenosine triphosphate and muscular contraction. Nature London 163: 320, 1949.
 95. Hill, A. V. The heat of activation and the heat of shortening in a muscle twitch. Proc. R. Soc. London Ser. B 136: 195–211, 1949.
 96. Hill, A. V. A challenge to biochemists. Biochim. Biophys. Acta 4: 4–11, 1950.
 97. Hill, A. V. The effect of load on the heat of shortening of muscle. Proc. R. Soc. London Ser. B 159: 297–318, 1964.
 98. Hill, A. V., and W. Hartree. The four phases of heat production of muscle. J. Physiol. London 54: 84–128, 1920.
 99. Hill, A. V., and J. V. Howarth. The reversal of chemical reactions in contracting muscle during an applied stretch. Proc. R. Soc. London Ser. B 151: 169–193, 1959.
 100. Hill, A. V., and R. C. Woledge. An examination of absolute values in myothermic measurements. J. Physiol. London 162: 311–333, 1962.
 101. Hill, D. K. The time course of the oxygen consumption of stimulated frog's muscle. J. Physiol. London 98: 207–227, 1940.
 102. Hill, D. K. The location of creatine phosphate in frog's striated muscle. J. Physiol. London 164: 31, 1962.
 103. Hill, D. K. The location of adenine nucleotide in the striated muscle of the toad. J. Cell Biol. 20: 435–458, 1964.
 104. Hill, L. A‐band length, striation spacing and tension change on stretch of active muscle. J. Physiol. London 266: 677–685, 1977.
 105. Himms‐Hagen, J. Cellular thermogenesis. Annu. Rev. Physiol. 38: 315–351, 1976.
 106. Hinkle, P. C, and M. L. Yu. The phosphorus/oxygen ratio of mitochondrial oxidative phosphorylation. J. Biol. Chem. 254: 2450–2455, 1979.
 107. Homsher, E., M. Irving, and A. Wallner. High‐energy phosphate metabolism and energy liberation associated with rapid shortening in frog skeletal muscle. J. Physiol. London 321: 423–436, 1981.
 108. Homsher, E., and C. J. Kean. Skeletal muscle energetics and metabolism. Annu. Rev. Physiol. 40: 93–131, 1978.
 109. Homsher, E., C. J. Kean, A. Wallner, and V. Garibian‐Sarian. The time‐course of energy balance in an isometric tetanus. J. Gen. Physiol. 73: 553–567, 1979.
 110. Homsher, E., and C. J. C. Kean. Unexplained enthalpy production in isometric contractions and its relation to intracellular calcium movements. In: The Regulation of Muscle Contraction: Excitation‐Contraction Coupling. New York: Academic, 1980, pp. 337–347.
 111. Homsher, E., W. F. H. M. Mommaerts, and N. V. Ricchiuti. Energetics of shortening muscles in twitches and tetanic contractions. J. Gen. Physiol. 62: 677–692, 1973.
 112. Homsher, E., W. F. H. M. Mommaerts, N. V. Ricchiuti, and A. Wallner. Activation heat, activation metabolism and tension‐related heat in frog semitendinosus muscles. J. Physiol. London 220: 601–625, 1972.
 113. Homsher, E., and J. A. Rall. Energetics of shortening muscles in twitches and tetani contractions. I. A reinvestigation of Hill's concept of shortening heat. J. Gen. Physiol. 62: 663–676, 1973.
 114. Homsher, E., J. A. Rall, A. Wallner, and N. V. Ricchiuti. Energy liberation and chemical change In frog skeletal muscle during single isometric tetanic contractions. J. Gen. Physiol. 65: 1–21, 1975.
 115. Hoppeler, H., D. Mathieu, R. Krauer, H. Cloasen, R. B. Armstrong, and E. R. Weibel. Distribution of mitochondria and capillaries in various muscles. Respir. Physiol. 44: 87–111, 1981.
 116. Hoult, D. I., S. J. W. Busby, D. G. Gadian, G. K. Radda, R. E. Richards, and P. J. Seeley. Observation of tissue metabolites using 31P nuclear magnetic resonance. Nature London 252: 285–287, 1974.
 117. Huxley, A. F. Muscle structure and theories of contraction. Prog. Biophys. Biophys. Chem. 7: 255–318, 1957.
 118. Huxley, A. F., and R. Niedergerke. Structural changes in muscle during contraction. Nature London 173: 971–973, 1954.
 119. Huxley, H., and J. Hanson. Changes in the cross‐striations of muscle during contraction and stretch and their structural interpretation. Nature London 173: 973–976, 1954.
 120. Infante, A. A., D. Klaupiks, and R. E. Davies. Adenosine triphosphate: changes in muscles doing negative work. Science 144: 1577–1578, 1964.
 121. Infante, A. A., D. Klaupiks, and R. E. Davies. Phosphorylcreatine consumption during single working contractions of isolated muscle. Biochim. Biophys. Acta 94: 504–515, 1965.
 122. Ingwall, J. S., C. D. Weiner, M. F. Morales, E. S. Davis, and F. E. Stockdale. Specificity of creatine in the control of muscle protein synthesis. J. Cell Biol. 63: 145–151, 1974.
 123. Jacobus, W. E., and J. S. Ingwall, (editors)., Heart Creatine Kinase. Baltimore, MD: Williams & Wilkins, 1980.
 124. Jacobus, W. E., and A. L. Lehninger. Creatine kinase of rat heart mitochondria. J. Biol. Chem. 248: 4803–4810, 1973.
 125. JÖBsis, F. F. Spectrophotometric studies on intact muscle. I. Components of the respiratory chain. J. Gen. Physiol. 46: 905–928, 1963.
 126. JÖBsis, F. F., and J. C. Duffield. Oxidative and glycolytic recovery metabolism in muscle. J. Gen. Physiol. 50: 1009–1047, 1967.
 127. Julian, F. J. The effect of calcium on the force‐velocity relation of briefly glycerinated frog muscle fibres. J. Physiol. London 218: 117–145, 1971.
 128. Kennedy, B. G., and P. Deweer. Strophanthidin‐sensitive sodium fluxes in metabolically poisoned frog skeletal muscle. J. Gen. Physiol. 68: 405–420, 1976.
 129. Klingenberg, M., and H. Rottenberg. Relation between the gradient of the ATP/ADP ratio and the membrane potential across the mitochondrial membrane. Eur. J. Biochem. 73: 125–130, 1977.
 130. Kodama, T., and R. C. Woledge. Enthalpy changes for intermediate steps of the ATP hydrolysis catalyzed by myosin subfragment‐1. J. Biol. Chem. 254: 6382–6386, 1979.
 131. Krebs, H. A., and R. L. Veech. Pyridine nucleotide control in Mitochondria. In: The Energy Level and Metabolic Control in Mitochondria, edited by S. Papa, J. M. Tager, E. Quagliariello, and E. C. Slater. Bari, Italy: Adriatica Editrice, 1969, p. 329–382.
 132. Kretzschmar, K. M., and D. R. Wilkie. A new approach to freezing tissues rapidly. J. Physiol. London 202: 66P–67P, 1969.
 133. Kretzschmar, K. M., and D. R. Wilkie. The use of the Peltier effect for simple and accurate calibration of thermoelectric devices. Proc. R. Soc. London Ser. B 190: 315–321, 1975.
 134. Kuby, S. A., L. Noda, and H. A. Lardy. Adenosinetriphosphate‐creatine transphosphorylase. I. Isolation of the crystalline enzyme from rabbit muscle. J. Biol. Chem. 209: 191–201, 1954.
 135. Kuby, S. A., L. Noda, and H. A. Lardy. Adenosinetriphosphate‐creatine transphosphorylase III. Kinetic studies. J. Biol. Chem. 210: 65–95, 1954.
 136. Kushmerick, M. J. Energy balance in muscle contraction: a biochemical approach. Curr. Top. Bioenerg. 6: 1–37, 1977.
 137. Kushmerick, M. J., T. Brown, and M. Crow. Rates of ATP: creatine phosphorytransferase reaction in skeletal muscle by 31P nuclear resonance spectroscopy (Abstract). Federation Proc. 39: 1934, 1980.
 138. Kushmerick, M. J., and R. E. Davies. The chemical energetics of muscle contraction. II. The chemistry, efficiency and power of maximally working sartorius muscles. Proc. R. Soc. London Ser. B 1174: 315–353, 1969.
 139. Kushmerick, M. J., R. E. Larson, and R. E. Davies. The chemical energetics of muscle contraction. I. Activation heat, heat of shortening and ATP utilization for activation‐relaxation processes. Proc. R. Soc. London Ser. B 174: 293–313, 1969.
 140. Kushmerick, M. J., and R. J. Paul. Aerobic recovery metabolism following a single isometric tetanus in frog sartorius muscle at 0°C. J. Physiol. London 254: 693–709, 1976.
 141. Kushmerick, M. J., and R. J. Paul. Relationship between initial chemical reactions and oxidative recovery metabolism for single isometric contractions of frog sartorius at 0°C. J. Physiol. London 254: 711–727, 1976.
 142. Kushmerick, M. J., and R. J. Paul. Chemical energetics in repeated contractions of frog sartorius muscle at 0°C. J. Physiol. London 267: 249–260, 1977.
 143. Kushmerick, M. J., and R. J. Podolsky. Ionic mobility in muscle cells. Science 166: 1297–1298, 1969.
 144. Lange, G. Über die Dephosphorylierung von Adenosinetriphosphat zu Adenosinediphosphat während der Kontraktionphase von Froschrectus‐Muskel. Biochem. Z. 326: 172, 1955.
 145. Lawrie, R. A. The activity of the cytochrome system in muscles and its relation to myoglobin. Biochem. J. 55: 298–305, 1953.
 146. Lawson, J. W. R., and R. L. Veech. Effects of pH and free Mg2+ on the Keq, of the creatine kinase reaction and other phosphate hydrolyses and phosphate transfer reactions. J. Biol. Chem. 254: 6528–6537, 1979.
 147. Lee, Y. P. 5'‐Adenylic acid deaminase. HI. Properties and kinetic studies. J. Biol. Chem. 227: 999–1007, 1957.
 148. Lehningeh, A. L., A. Vercesi, and E. A. Bababunmi. Regulation of Ca++ release from mitochondria by the oxidation‐reduction state of pyridine nucleotides. Proc. Natl. Acad. Sci. USA 75: 1690–1694, 1978.
 149. Levy, R. M., Y. Umazume, and M. J. Kushmerick. Ca2+ dependence of tension and ADP production in segments of chemically skinned muscle fibers. Biochim. Biophys. Acta 430: 352–365, 1976.
 150. Lipmann, F. Metabolic generation and utilization of phosphate band energy. Adv. Enzymol. Relat. Areas Mol. Biol. 1: 99–162, 1941.
 151. Lohmann, K. Über die enzymatische Aufspalturg der Kreatinephosphorsäure; zugleich ein Beitrag zum Chemismus der Muskelkontraktion. Biochem. Z. 271: 264–277, 1934.
 152. Lowenstehj, J. M. Ammonia production in muscle and other tissues: the purine nucleotide cycle. Physiol. Rev. 52: 382–414, 1972.
 153. Lowry, O. H., and J. V. Passonneau. The relationships between substrates and enzymes of glycolysis in brain. J. Biol. Chem. 239: 31–42, 1964.
 154. Lowry, O. H., and J. V. Passonneau. A Flexible System of Enzymatic Analysis. New York: Academic, 1972.
 155. Lowry, O. H., J. V. Passonneau, F. X. Hasselberger, and D. W. Schulz. Effect of ischemia on known substrates and cofactors of the glycolytic pathway in brain. J. Biol. Chem. 239: 18–30, 1964.
 156. Loxdale, H. P. A method for the continuous assay of picomole quantities of ADP released from glycerol‐extracted skeletal muscle fibres on MgATP activation. J. Physiol. London 247: 71–89, 1975.
 157. Luff, A. R., and U. Proske. Properties of motor units of the frog sartorius muscle. J. Physiol. London 258: 673–685, 1976.
 158. Lundsgaard, E. Untersuchungen über Muskelkontraktion ohne Milchsaure. Biochem. Z. 217: 162–177, 1930.
 159. Lundsgaard, E. The biochemistry of muscle. Annu. Rev. Biochem. 7: 377–398, 1938.
 160. Lundsgaard, E. The ATP content of resting and active muscle. Proc. R. Soc. London Ser. B 137: 73–76, 1950.
 161. Maclennan, D. H., and P. C. Holland. Calcium transport in sarcoplasmic reticulum. Annu. Rev. Biophys. Bioeng. 4: 377–404, 1975.
 162. Mahler, M. Diffusion and consumption of oxygen in the resting frog sartorius muscle. J. Gen. Physiol. 71: 533–557, 1978.
 163. Mahler, M. Kinetics of oxygen consumption after a single isometric tetanus of frog sartorius muscle at 20°C. J. Gen. Physiol. 71: 559–580, 1978.
 164. Marban, E., T. J. Rink, R. W. Tsien, and R. Y. Tsien. Free calcium in heart muscle at rest and during contraction measured with Ca++‐sensitive microelectrodes. Nature London 286: 845–850, 1980.
 165. Maréchal, G. Le Metabolisme de la phosphorylcreatine et de l'adenosine triphosphate durant la contraction musculaire. Brussels: Arscia, 1962.
 166. Marston, S. B., and R. T. Tregear. Evidence for a complex between myosin and ADP in relaxed muscle fibres. Nature London New Biol. 235: 23–24, 1972.
 167. Martonosi, A., and R. Feretos. Sarcoplasmic reticulum. II. Correlation between adenosine triphosphatase activity and Ca++ uptake. J. Biol. Chem. 239: 659–668, 1964.
 168. Mcgdlvery, R. W., and T. W. Murray. Calculated equilibria of phosphocreatine and adenosine phosphates during utilization of high energy phosphate by muscle. J. Biol. Chem. 249: 5845–5850, 1974.
 169. Mela, L. Mechanism and physiological significance of calcium transport across mammalian mitochondrial membranes. In: Current Topics in Membranes and Transport, edited by F. Bronner and A. Kleinzeller. New York: Academic, 1977, vol. 9, p. 321–366.
 170. Mendelson, R. A., and P. Cheung. Muscle crossbridges: absence of direct effect of calcium on movement away from the thick filaments. Science 194: 190–192, 1976.
 171. Meyer, R. A., J. Ghaoteaux, and R. L. Terjung. Histochemical demonstration of differences in AMP deaminase activity in rat skeletal muscle fibers. Experientia 36: 676–677, 1980.
 172. Meyer, R. A., and R. L. Terjung. Differences in ammonia and adenylate metabolism in contracting fast and slow muscle. Am. J. Physiol. 237 (Cell Physiol. 6): C111–C118, 1979.
 173. Meyer, R. A., and R. L. Terjung. AMP deamination and IMP reamination in working skeletal muscle. Am. J. Physiol. 239 (Cell Physiol. 8): C32–C38, 1980.
 174. Meyerhof, O., and W. Schulz. Über die Energieverhältnisse bei der enzymatischen Milchsäurebildung und der Synthese der Phosphagene. Biochem. Z. 281: 292–305, 1935.
 175. Meyerhof, O., W. Schulz, and P. Schuster. Über die enzymatische Synthese der Kreatinephosphosäure und die biologische Reaktionsform des Zuckers. Biochem. Z. 293: 309–337, 1937.
 176. Millikan, G. A. Experiments on muscle hemoglobin in vivo; the instantaneous measurement of muscle metabolism. Proc. R. Soc. London Ser. B 123: 218–241, 1939.
 177. Mommaerts, W. F. H. M. Energetics of muscular contraction. Physiol. Rev. 49: 427–508, 1969.
 178. Mommaerts, W. F. H. M., and J. C. Rupp. Dephosphorylation of adenosinetriphosphate in muscular contraction. Nature London 158: 957, 1951.
 179. Mommaerts, W. F. H. M., K. Vegh, and E. Homsher. Activation of Phosphorylase in frog muscle as determined by contractile activity. J. Gen. Physiol. 66: 657–669, 1975.
 180. Munch‐Petersen, A. Dephosphorylation of adenosinetriphosphate during the rising phase of a muscle twitch. Acta Physiol. Scand. 29: 202–219, 1953.
 181. Natori, R. The property and contraction process of isolated myofibrils. Jikeikai Med. J. 1: 119–126, 1954.
 182. Nichols, D. G. The bioenergetics of brown adipose tissue mitochondria. FEBS Lett. 61: 103–110, 1976.
 183. Nichols, D. G. Hamster brown adipose mitochondria. Eur. J. Biochem. 62: 223–228, 1976.
 184. Nihei, T., R. A. Mendelson, and J. Botts. The site of force generation in muscle contraction as deduced from fluorescence polarization studies. Proc. Natl. Acad. Sci. USA 71: 274–277, 1974.
 185. Noda, L. Adenosine triphosphate‐adenosine monophosphate transphosphorylase. III. Kinetic studies. J. Biol. Chem. 232: 237, 1958.
 186. Noda, L., S. A. Kuby, and H. A. Lardy. Adenosinetriphosphate‐creatine transphosphorylase. II. Homogeneity and physiochemical properties. J. Biol. Chem. 209: 203–210, 1954.
 187. Noda, L., S. A. Kuby, and H. A. Lardy. Adenosinetriphosphate‐creatine transphosphorylase. IV. Equilibrium studies. J. Biol. Chem. 210: 83–95, 1954.
 188. Owen, C. S., and D. F. Wilson. Control of respiration by mitochondrial phosphorylation state. Arch. Biochem. Biophys. 161: 581–591, 1974.
 189. Page, E. Quantitative ultrastructural analysis in cardiac membrane physiology. Am. J. Physiol. 235 (Cell Physiol. A): C147–C158, 1978.
 190. Parnas, J. K., and W. Mozolowski. Über die Ammoniakgehalt und die Ammoniakbildung in Muskel und deren Zusammenhang mit Funktion und Zustandsanderung. Biochem. Z. 184: 399–441, 1927.
 191. Paul, R. J., and M. J. Kushmerick. Apparent P/O ratio and chemical energy balance in frog sartorius muscle in vitro. Biochim. Biophys. Acta 347: 483–490, 1974.
 192. Peachey, L. D. The sarcoplasmic reticulum and transverse tubules of the frog's sartorius. J. Cell Biol. 25: 209–231, 1965.
 193. Peter, J. B., R. J. Barnard, V. R. Edgerton, C. A. Gillespie, and K. E. Stengel. Metabolic profiles of three fiber types of skeletal muscle in guinea pigs and rabbits. Biochemistry 11: 2627–2633, 1972.
 194. Pfaff, E., and M. Klingenberg. Adenosine nucleotide translocation of mitochondria. Eur. J. Biochem. 6: 66–70, 1968.
 195. Rall, J. A. Effects of temperature on tension, tension‐dependent heat, and activation heat in twitches of frog skeletal muscle. J. Physiol. London 291: 265–275, 1979.
 196. Rall, J. A., E. Homsher, A. Wallner, and W. F. H. M. Mommaerts. A temporal dissociation of energy liberation and high energy phosphate splitting during shortening in frog skeletal muscles. J. Gen Physiol. 68: 13–27, 1976.
 197. Robertson, S. P., J. D. Johnson, and J. D. Potter. The time course of Ca++ exchange with calmodulin, troponin, parvalbumin and myosin in response to transient increases in Ca++. Biophys. J. 34: 559–569, 1981.
 198. Romanul, F. C. A. Capillary supply and metabolism of muscle fibers. Arch. Neurol. 12: 497–509, 1965.
 199. Roos, A. Intracellular pH and buffering power of rat muscle. Am. J. Physiol. 221: 182–188, 1971.
 200. Roos, A. Intracellular pH and distribution of weak acids across cell membranes. A study of D‐ and L‐lactate and of DMO in rat diaphragm. J. Physiol. London 249: 1–25, 1975.
 201. Rose, I. A. The state of magnesium in cells as estimated from the adenylate kinase equilibrium. Proc. Natl. Acad. Sci. USA. 61: 1079–1086, 1968.
 202. Saks, V. A., G. B. Chernousova, R. Vetter, V. N. Smirnov, and E. I. Chazov. Kinetic properties and the functional role of particulate mm‐isoenzyme of creatine Phosphokinase bound to heart muscle myofibrils. FEBS Lett. 62: 293–296, 1976.
 203. Sandberg, J. A., and F. D. Carlson. The length dependence of phosphorylcreatine hydrolysis during an isometric tetanus. Biochem. Z. 345: 212–231, 1966.
 204. Saris, N.‐E., and K. E. D. Akerman. Uptake and release of bivalent cations in mitochondria. Curr. Top. in Bioenerg. 10: 103–179, 1980.
 205. Scholte, H. R. On the triple localization of creatine kinase in heart and skeletal muscle cells of the rat: evidence for the existence of myofibrillar and mitochondrial isoenzymes. Biochim. Biophys. Acta 305: 413–427, 1973.
 206. Scopes, R. K. Studies with a reconstituted muscle glycolytic system. The rate and extent of creatine phosphorylation by anaerobic glycolysis. Biochem. J. 134: 197–208, 1973.
 207. Scopes, R. K. Studies with a reconstituted glycolytic system. The anaerobic glycolytic response to simulated tetani contraction. Biochem. J. 138: 119–123, 1974.
 208. Skoog, C, U. Kromer, R. W. Mitchell, J. Hoogstraten, and N. L. Stephens. Characterization of frog muscle mitochondria. Am. J. Physiol. 234 (Cell Physiol. 3): C1–C6, 1978.
 209. Smith, I. C. H. Energetics of activation frog and toad muscle. J. Physiol. London 220: 583–599, 1972.
 210. Solandt, D. Y. The effect of potassium on the excitability and resting metabolism of frog's muscle. J. Physiol. London 86: 162–170, 1936.
 211. 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.
 212. Sréter, F. A. Temperature, pH and seasonal dependence of Ca‐uptake and ATPase activity of white and red muscle microsomes. Arch. Biochem. Biophys. 134: 25–33, 1969.
 213. Steinberg, I. Z., A. Optalka, and A. Katchalsky. Mechanochemical engines. Nature London 210: 568–571, 1966.
 214. Sugden, P. H., and E. A. Newsholme. The effects of ammonium, inorganic phosphate and potassium ions on the activity of phosphofructokinase from muscle and nervous tissue of vertebrates and invertebrates. Biochem. J. 150: 113–122, 1975.
 215. Takashi, R., and S. Putnam. A fluorimetric method for continuously assaying ATPase: application to small specimens of glycerol‐extracted muscle fibers. Anal. Biochem. 92: 375–382, 1979.
 216. Thames, M. D., L. E. Teichholz, and R. J. Podolsky. Ionic strength and the contraction kinetics of skinned muscle fibers. J. Gen. Physiol. 63: 509–530, 1974.
 217. Thayer, W. S., and P. C. Hinkle. Stoichiometry of adenosine triphosphate‐driven proton translocation in bovine heart submitochondrial particles. J. Biol. Chem. 248: 5395–5402, 1973.
 218. Thomas, R. C. Electrogenic sodium pump in nerve and muscle cells. Physiol. Rev. 52: 563–594, 1972.
 219. Veech, R. L., J. W. R. Lawson, N. W. Cornell, and H. A. Krebs. Cytosolic phosphorylation potential. J. Biol. Chem. 254: 6538–6547, 1979.
 220. Venosa, R. A. Inward movement of sodium ions in resting and stimulated frog's sartorius muscle. J. Physiol. London 241: 155–173, 1974.
 221. Vial, C, C. Godinot, and D. Gautheron. Creatine kinase (E.C.2.7.3.2.) in pig heart mitochondria. Properties and role in phosphate potential regulation. Biochimie 54: 843–852, 1972.
 222. Vincent, A., and J. McD. Blair. The coupling of the adenylate kinase and creatine kinase equilibria. Calculation of substrate and feedback signal levels in muscle. FEBS Lett. 7: 239–244, 1970.
 223. Wajzer, J., R. Weber, J. Lerique, and J. Nekhorochiff. Reversible degradation of adenosine triphosphate to inosine acid during a single muscle twitch. Nature London 178: 1287–1288, 1956.
 224. Weber, A. Regulatory mechanisms of the calcium transport system of fragmented rabbit sarcoplasmic reticulum. I. The effect of accumulated calcium on transport and adenosine triphosphate hydrolysis. J. Gen. Physiol. 57: 50–63, 1971.
 225. Wikström, M., and K. Krab. Respiration‐linked H+ translocation in mitochondria: stoichiometry and mechanism. Curr. Top. Bioenerg. 10: 51–101, 1980.
 226. Wilkie, D. R. Thermodynamics and the interpretation of biological heat measurements. Prog. Biophys. Biophys. Chem. 10: 260–298, 1960.
 227. Wilkie, D. R. Heat work and phosphorylcreatine breakdown in muscle. J. Physiol. London 195: 157–183, 1968.
 228. Wilson, D. F., M. Erecinska, C. Drown, and I. A. Silver. Effect of oxygen tension on cellular energetics. Am. J. Physiol. 233 (Cell Physiol. 2): C135–C140, 1977.
 229. Wilson, D. F., M. Stubbs, N. Ohsino, and M. Erecinska. Thermodynamic relationships between the mitochondrial oxidation‐reduction reactions and cellular ATP levels in ascites tumor cells and perfused rat liver. Biochemistry 13: 5305–5311, 1974.
 230. Wilson, D. F., M. Stubbs, R. L. Veech, M. Erecinska, and H. A. Krebs. Equilibrium relations between the oxidation‐reduction reactions and the ATP triphosphate synthesis in suspensions of isolated liver cells. Biochem. J. 140: 57–64, 1974.
 231. Winegrad, S. The intracellular site of calcium activation of contraction in frog skeletal muscle. J. Gen. Physiol. 55: 77–88, 1970.
 232. Wittenberg, J. B. Myoglobin‐facilitated oxygen diffusion: role of myoglobin in oxygen entry into muscle. Physiol. Rev. 50: 559–636, 1970.
 233. Woledge, R. C. The thermoelastic effect of change of tension in active muscle. J. Physiol. London 155: 187–208, 1961.
 234. Woledge, R. C. The energetics of tortoise muscle. J. Physiol. London 197: 685–707, 1968.
 235. Woledge, R. C. Heat production and chemical change in muscle. In: Progress in Biophysics and Molecular Biology, edited by J.A.V. Butler and D. Noble. New York: Pergamon, 1971, vol. 22, p. 37–72.
 236. Woledge, R. C. In vitro calorimetric studies relating to the interpretation of muscle heat experiments. Cold Spring Harbor Symp. Quant. Biol. 37: 629–634, 1972.
 237. Wollenberger, E., G. Krause, and B. E. Wahler. Orthophosphat und Phosphokreatingeholt des Herzmuskels. Naturwissenschaften 45: 294, 1958.
 238. Yagi, N., and I. Matsubara. Myosin heads do not move on activation in highly stretched vertebrate striated muscle. Science 207: 307–308, 1980.

Contact Editor

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

* Required Field

How to Cite

Martin J. Kushmerick. Energetics of Muscle Contraction. Compr Physiol 2011, Supplement 27: Handbook of Physiology, Skeletal Muscle: 189-236. First published in print 1983. doi: 10.1002/cphy.cp100107