Comprehensive Physiology Wiley Online Library

Hydrolytic Transformation of Environmental Pollutants

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Ester Hydrolysis
2 Organophosphorus Triesters
2.1 Phosphorylphosphatases (Fluorophosphatases)
2.2 Arylesterases
2.3 Carboxylesterases
2.4 Carboxyamidase
2.5 Other Hydrolytic Mechanisms
3 Carbamic Acid Esters
4 Pyrethyroid Ester Insecticides
5 Herbicide Esters
6 Phthalic Acid Esters
References
 1. Abernathy, C. O., and J. E. Casida. Pyrethroid insecticides. Esterase cleavage in relation to selective toxicity. Science 179: 1235-1236, 1973.
 2. Abernathy, C. O., K. Ueda, J. L. Engel, L. C. Gaughan, and J. E. Casida. Substrate‐specificity and toxicological significance of pyrethroid‐hydrolyzing esterases of mouse liver microsomes. Pesticide Biochem. Physiol. 3: 300-311, 1973.
 3. Adie, P. A., and J. Tuba. The intracellular localization of liver and kidney sarinase. Can. J. Biochem. Physiol. 36: 21-24, 1958.
 4. Albro, P. W., and R. O. Thomas. Enzymatic hydrolysis of di‐(2‐ethylhexyl) phthalate by lipases. Biochim. Biophys. Acta 360: 380-390, 1973.
 5. Albro, P. W., R. Thomas, and L. Fishbein. Metabolism of diethylhexyl phthalate by rats. Isolation and characterization of the urinary metabolites. J. Chromatog. 76: 321-330, 1973.
 6. Aldridge, W. N. Serum esterases. 1. Two types of esterase (A and B) hydrolyzing p‐nitrophenyl acetate, propionate and butyrate and a method for their determination. Biochem. J. 53: 110-117, 1953.
 7. Aldridge, W. N. Serum esterases. 2. An enzyme hydrolyzing diethyl p‐nitrophenyl phosphate (E 600) and its identity with the A‐esterase of mammalian serum. Biochem. J. 53: 117-124, 1953.
 8. Aldridge, W. N. The nature of the reaction of organophosphorus compounds and carbamates with esterases. Bull. World Health Organ. 44: 25-30, 1971.
 9. Aldridge, W. N., and E. Reiner. Enzyme Substrates as Inhibitors. Interaction of Esterases With Esters of Organophosphorus and Carbamic Acids. New York: Am. Elsevier, 1972.
 10. Augustsyn, R. C., J. De Jersey, E. C. Webb, and B. Zerher. On the homology of the active‐site peptides of liver carboxylesterases. Biochim. Biophys. Acta 171: 128-137, 1969.
 11. Augustinsson, K.‐B. The enzymic hydrolysis of organophosphorus compounds. Biochim. Biophys. Acta 13: 303-304, 1954.
 12. Augustinsson, K.‐B. Electrophoresis studies on blood plasma esterases. I. Mammalian plasmata. Acta Chem. Scand. 13: 571-592, 1959.
 13. Augustinsson, K.‐B. Electrophoresis studies on blood plasma esterases. II. Avian, reptilian, amphibian and piscine plasmata. Acta Chem. Scand. 13: 1081-1096, 1959.
 14. Augustinsson, K.‐B. Electrophoresis studies on blood plasma esterases. III. Conclusions. Acta Chem. Scand. 13: 1097-1105, 1959.
 15. Augustinsson, K.‐B. Multiple forms of esterase in vertebrate blood plasma. Ann. NY Acad. Sci. 94: 844-860, 1961.
 16. Augustinsson, K.‐B. Arylesterases. J. Histochem. Cytochem. 12: 744-747, 1964.
 17. Augustinsson, K.‐B., and J. E. Casida. Enzymic hydrolysis of N: N‐dimethylcarbamoyl fluoride. Biochem. Pharmacol. 3: 60-67, 1959.
 18. Augustinsson, K.‐B., and G. Ekedahl. On the specificity of arylesterases. Acta Chem. Scand. 16: 240-241, 1962.
 19. Augustinsson, K.‐B., and G. Heimburger. Enzymatic hydrolysis of organophosphorus compounds. I. Occurrence of enzymes hydrolyzing dimethyl‐amido‐ethoxy‐phosphoryl cyanide (Tabun). Acta Chem. Scand. 8: 753-761, 1954.
 20. Augustinsson, K.‐B., and G. Heimburger. Enzymatic hydrolysis of organophosphorus compounds. IV. Specificity studies. Acta Chem. Scand. 8: 1533-1541, 1954.
 21. Augustinsson, K.‐B., and G. Heimburger. Enzymatic hydrolysis of organophosphorus compounds. VI. Effects of metal ions on the phosphorylphosphatases of human serum and swine kidney. Acta Chem. Scand. 9: 383-392, 1955.
 22. Baron, R. L., J. L. Casterline, and O. G. Fitzhugh. Specificity of carbamate‐induced esterase inhibition in mice. Toxicol. Appl. Pharmacol. 6: 402-410, 1964.
 23. Bergmann, F., R. Segal, and S. Rimon. A new type of esterase in hog‐kidney extract. Biochem. J. 67: 481-486, 1957.
 24. Bridges, P. M. Absorption and metabolism of [14C]allethrin by the adult housefly, Musca domestica L. Biochem. J. 66: 316-320, 1957.
 25. Bull, D. L., and D. A. Lindquist. Metabolism of 3‐hydroxy‐N,N‐dimethyl crotonamide dimethyl phosphate by cotton plants, insects and rats. J. Agr. Food Chem. 12: 310-317, 1964.
 26. Bull, D. L., and D. A. Linquist. Metabolism of 3‐hydroxy‐N‐methyl‐cis‐crotonamide dimethyl phosphate (Azodrin) by insects and rats. J. Agr. Food Chem. 14: 105-109, 1966.
 27. Casida, J. E. Mode of action of carbamates. In: Annual Review of Entomology, edited by R. F. Smith. Palo Alto, Calif.: Ann. Rev., 1963, p. 39-58.
 28. Casida, J. E. (editor). Pyrethrum, the Natural Insecticide. New York: Academic Press, 1973.
 29. Casida, J. E., and K.‐B. Augustinsson. Reaction of plasma albumin with 1‐naphthyl N‐methylcarbamate and certain other esters. Biochim. Biophys. Acta 36: 411-426, 1959.
 30. Casida, J. E., E. C Kimmel, M. Elliott, and N. F. Janes. Oxidative metabolism of pyrethrins in mammals. Nature 230: 326-327, 1971.
 31. Casida, J. E., L. McBride, and R. P. Niedermeier. Metabolism of 2,2‐dichlorovinyl dimethyl phosphate in relation to residues in milk and mammalian tissues. J. Agr. Food Chem. 10: 370-377, 1962.
 32. Chamberlain, R. W. An investigation on the action of piperonyl butoxide with pyrethrum. Am. J. Hyg. 52: 153-183, 1950.
 33. Chamberlain, W. F., P. E. Gatterdam, and D. E. Hopkins. The metabolism of P32‐labeled dimethoate in sheep. J. Econ. Entomol. 54: 733-740, 1961.
 34. Chambon, P., M. Riotte, M. Daudon, R. Chambon‐Mougenot, and J. Bringuier. Etude du métabolisme des phthalates de dibutyle et de diéthyle chez le rat. Compt. Rend. 273: 2165-2168, 1971.
 35. Chen, P. R. S., and W. C. Dauterman. Studies on the toxicity of dimethoate analogs and their hydrolysis by sheep liver amidase. Pesticide Biochem. Physiol. 1: 340-348, 1971.
 36. Chen, P. R., W. P. Tucker, and W. C. Dauterman. Structure of biologically produced malathion monoacid. J. Agr. Food Chem. 17: 86-90, 1969.
 37. Chiu, Y. C., A. Hassan, F. E. Guthrie, and W. C. Dauterman. Studies on a series of branched‐chain analogs of diethyl malathion and malaoxon with regard to toxicity and in vitro enzymatic reactions. Toxicol. Appl. Pharmacol. 12: 219-228, 1968.
 38. Cochrane, D. R., J. D. Pope, H. P. Nicholson, and G. W. Bailey. The persistence of silvex in water and hydrosoils. Water Resources Res. 3: 517-523, 1967.
 39. Cohen, J. A., R. A. Oosterbaan, and M. G. P. J. Warringa. The turnover number of ali‐esterase, pseudo‐ and true cholinesterase and the combination of these enzymes with diisopropylfluorophosphate. Biochim. Biophys. Acta 18: 228-235, 1955.
 40. Cohen, J. A., R. A. Oosterbaan, H. S. Jansz, and F. Berends. The active site of esterases. J. Cellular Comp. Physiol. 54: 231-244, 1959.
 41. Cohen, J. A., and M. G. P. J. Warringa. Purification and properties of dialkylfluorophosphatase. Biochim. Biophys. Acta 26: 29-39, 1957.
 42. Cohen, S. D., J. E. Callaghan, and S. D. Murphy. Investigation of multiple mechanisms for potentiation of malaoxon's anticholinesterase action by triorthotolyl phosphate. Proc. Soc. Exptl. Biol. Med. 141: 906-910, 1972.
 43. Cohen, S. D., and S. D. Murphy. Comparative potentiation of malathion by triorthotolyl phosphate in four classes of vertebrates. Toxicol. Appl. Pharmacol. 16: 701-708, 1970.
 44. Cohen, S. D., and S. D. Murphy. Carboxylesterase inhibition as an indicator of malathion potentiation in mice. J. Pharmacol. Exptl. Therap. 176: 733-742, 1971.
 45. Cohen, S. D., and S. D. Murphy. Inactivation of malaoxon by mouse liver. Proc. Soc. Exptl. Biol. Med. 139: 1385-1389, 1972.
 46. Cook, J. W., J. R. Blake, and G. Yip. Malathionase. I. Activity and inhibition. J. Assoc. Offic. Agr. Chemists 41: 399-407, 1958.
 47. Cook, J. W., and G. Yip. Malathionase. II. Identity of a malathion metabolite. J. Assoc. Offic. Agr. Chemists 41: 407-411, 1958.
 48. Crafts, A. S. Evidence for hydrolysis of 2,4‐D during absorption by plants. Weeds 8: 19-25, 1960.
 49. Dauterman, W. C., and A. R. Main. Relationship between acute toxicity and in vitro inhibition and hydrolysis of a series of carbalkoxy homologs of malathion. Toxicol. Appl. Pharmacol. 9: 408-418, 1966.
 50. Dicowsky, L., and A. Morello. Glutathione‐dependent degradation of 2,2‐dichlorovinyl dimethyl phosphate (DDVP) by the rat. Life Sci., Part 2 10: 1031-1037, 1971.
 51. Dorough, H. W., and J. E. Casida. Nature of certain carbamate metabolites of the insecticide Sevin. J. Agr. Food Chem. 12: 294-304, 1964.
 52. Eason, L. H., and E. Stedman. Studies on the relationship between chemical constitution and physiological action. V. Molecular dissymmetry and physiological activity. Biochem. J. 27: 1257-1266, 1933.
 53. Ecobichon, D. J. Relative amounts of hepatic and renal carboxylesterases in mammalian species. Res. Commun. Chem. Pathol. Pharmacol. 3: 629-636, 1972.
 54. Ecobichon, D. J., and W. Kalow. Some properties of the soluble esterases of human liver. Can. J. Biochem. Physiol. 39: 1329-1332, 1961.
 55. Ecobichon, D. J., and W. Kalow. Properties and classification of the soluble esterases of human liver. Biochem. Pharmacol. 11: 573-583, 1962.
 56. Ecobichon, D. J., and W. Kalow. Action of organophosphorus compounds upon esterases of human liver. Can. J. Biochem. Physiol. 41: 1537-1546, 1963.
 57. Edelfrawi, M. E., and W. M. Hoskins. Relation of the rate of penetration and metabolism to the toxicity of sevin to three insect species. J. Econ. Entomol. 54: 401-405, 1961.
 58. Elliott, M. The relationship between the structure and the activity of pyrethroids. Bull. World Health Organ. 44: 315-324, 1971.
 59. Erdös, E. G., and L. E. Boggs. Hydrolysis of paraoxon in mammalian blood. Nature 190: 716-717, 1961.
 60. Erdös, E. G., C. R. Debay, and M. P. Westerman. Activation and inhibition of the arylesterase of human serum. Nature 184: 430-431, 1959.
 61. Erdös, E. G., C. R. Debay, and M. P. Westerman. Arylesterases in blood: effect of calcium and inhibitors. Biochem. Pharmacol. 5: 173-186, 1960.
 62. Erdös, E. G., and J. A. Laswick. Arylesterases in blood: Irreversible inactivation of the plasma enzyme. Biochem. Pharmacol. 8: 375-381, 1961.
 63. Fest, C., and K.‐J. Schmidt. The Chemistry of Organophosphorus Pesticides. New York: Springer‐Verlag, 1973.
 64. Fukunaga, K., J. Fukami, and T. Shishido. The in vitro metabolism of organophosphorus insecticides by tissue homogenates from mammals and insects. In: Residue Reviews, edited by F. A. Gunther. New York: Springer‐Verlag, 1969, vol. 25, p. 223-249.
 65. Fukuto, T. R., and R. L. Metcalf. Metabolism of insecticides in plants and animals. Ann. NY Acad. Sci. 160: 97-111, 1969.
 66. Goldstein, A. The mechanism of enzyme‐inhibitorsubstrate reactions. Illustrated by the cholinesterasephysostigmine‐acetylcholine system. J. Gen. Physiol. 27: 529-580, 1944.
 67. Goldstein, A. Properties and behaviors of purified human plasma cholinesterase. III. Competitive inhibition by prostigmine and other alkaloids with special reference to differences in kinetic behavior. Arch. Biochem. Biophys. 34: 169-188, 1951.
 68. Goldstein, A., and R. E. Hamslisch. Properties and behaviors of purified human plasma cholinesterase. IV. Enzymatic destruction of the inhibitors prostigmine and physostigmine. Arch. Biochem. Biophys. 35: 12-22, 1952.
 69. Goldstein, A., O. Krayer, M. A. Root, G. H. Acheson, and M. E. Doherty. Plasma neostigmine levels and cholinesterase inhibition in dogs and myasthenic patients. J. Pharmacol. Exptl. Therap. 96: 56-85, 1949.
 70. Goutier, R. Étude électrophorétique des estérases sériques et de la fixation du DF32P dans le sérum chez le lapin et le cobaye. Biochim. Biophys. Acta 19: 524-534, 1955.
 71. Guthrie, F. E., R. J. Monroe, and C. O. Abernathy. Response of the laboratory mouse to selection for resistance to insecticides. Toxicol. Appl. Pharmacol. 18: 92-101, 1971.
 72. Hassan, A., S. M. A. D. Zayed, and M. R. E. Bahig. Metabolism of organophosphorus insecticides. XI. Metabolic fate of dimethoate in the rat. Biochem. Pharmacol. 18: 2429-2438, 1969.
 73. Heath, D. F. Organophosphorus Poisons. Anticholinesterases and Related Compounds. New York: Pergamon Press, 1961.
 74. Hodgson, E., and J. E. Casida. Mammalian enzymes involved in the degradation of 2,2‐dichlorovinyl dimethyl phosphate. J. Agr. Food Chem. 10: 208-214, 1962.
 75. Hogan, J. W., and C. O. Knowles. Degradation of organophosphates by fish liver phosphatases. J. Fisheries Res. Board Can. 25: 1571-1579, 1968.
 76. Hollingworth, R. M. Comparative metabolism and selectivity of organophosphate and carbamate insecticides. Bull. World Health Organ. 44: 155-170, 1971.
 77. Holmstedt, B. Pharmacology of organophosphorus cholinesterase inhibitor. Pharmacol. Rev. 11: 567-688, 1959.
 78. Huggins, C., and J. Lapides. Chromogenic substrates. IV. Acyl esters of p‐nitrophenol as substrates for the colorimetric determination of esterases. J. Biol. Chem. 170: 467-482, 1947.
 79. Hutson, D. H., D. Blair, E. C. Hoadley, and B. A. Pickering. The metabolism of 14C‐Vapona in rats after administration by oral and inhalation routes. Toxicol. Appl. Pharmacol. 19: 378, 1971.
 80. Hutson, D. H., and E. C. Hoadley. The comparative metabolism of [14C‐vinyl]dichlorvos in animals and man. Arch. Toxikol. 30: 9-18, 1972.
 81. Hutson, D. H., and E. C. Hoadley. The metabolism of [14C‐methyl]dichlorvos in the rat and mouse. Xenobiotica 2: 107-116, 1972.
 82. Hutson, D. H., E. C. Hoadley, and B. A. Pickering. The metabolic fate of [vinyl‐1‐14C]dichlorvos in the rat after oral and inhalation exposure. Xenobiotica 1: 593-611, 1971.
 83. International Union of Biochemistry. Enzyme Nomenclature. Amsterdam: Elsevier, 1965.
 84. Jaeger, R. J., and R. J. Rubin. Plasticizers from plastic devices: extraction, metabolism and accumulation by biological systems. Science 170: 460-462, 1970.
 85. Johnsen, R. E., and P. A. Dahm. Activation and degradation efficiencies of liver microsomes from eight vertebrate species using organophosphates as substrates. J. Econ. Entomol. 59: 1437-1442, 1966.
 86. Johnson, M. K., and R. Lauwerys. Protection by some carbamates against the delayed neurotoxic effects of diisopropyl‐fluorophosphate. Nature 222: 1066-1067, 1969.
 87. Karczmar, A. G., O. Awad, and K. Blachut. Toxicity arising from joint intravenous administration of EPN and malathion to dogs. Toxicol. Appl. Pharmacol. 4: 133-147, 1962.
 88. Kearney, P. C. Purification and properties of an enzyme responsible for hydrolyzing phenylcarbamates. J. Agr. Food Chem. 13: 561-564, 1965.
 89. Knaak, J. B., and L. J. Sullivan. Metabolism of carbaryl in the dog. J. Agr. Food Chem. 15: 1125-1126, 1967.
 90. Knaak, J. B., M. J. Tullant, S. J. Kozbelt, and L. J. Sullivan. The metabolism of carbaryl in man, monkey, pig, and sheep. J. Agr. Food Chem. 16: 465-470, 1968.
 91. Kojima, K., and R. D. O'Brien. Paraoxon hydrolyzing enzymes in rat liver. J. Agr. Food Chem. 16: 574-584, 1968.
 92. Krishna, J. G., and J. E. Casida. Fate in rats of radiocarbon from ten variously labeled methyl and dimethylcrbamate‐14C insecticide chemicals and their hydrolysis products. J. Agr. Food Chem. 14: 98-105, 1966.
 93. Krueger, H. R., and J. E. Casida. Hydrolysis of certain organophosphate insecticides by housefly enzymes. J. Econ. Entomol. 54: 239-243, 1961.
 94. Krueger, H. R., and R. D. O'Brien. Relation between metabolism and differential toxicity of malathion in insects and mice. J. Econ. Entomol. 52: 1063-1067, 1959.
 95. Ku, T.‐Y. and J. L. Bishop. Penetration, excretion and metabolism of carbaryl in susceptible and resistant German cockroaches. J. Econ. Entomol. 60: 1328-1332, 1967.
 96. Lauwerys, R. R., and S. D. Murphy. Comparison of assay methods for studying O,O‐diethyl, O‐p‐nitrophenylphosphate (paraoxon) detoxication in vitro. Biochem. Pharmacol. 18: 789-800, 1969.
 97. Lauwerys, R. R., and S. D. Murphy. Interaction between paraoxon and tri‐o‐tolyl phosphate in rats. Toxicol. Appl. Pharmacol: 14: 348-357, 1969.
 98. Lee, D. H. K., and H. L. Falk (editors). Perspective on PAEs. In: Environ. Health Perspectives No. 3, Jan. 1973, p. 1-182. (U.S. Dept. Health, Educ., and Welfare Publ. No. NIH‐73‐218).
 99. Lichtenstein, E. P., T. W. Fuhremann, A. A. Hochberg, R. N. Zahlten, and F. W. Stratman. Metabolism of [14C]parathion and paraoxon with fractions and subfractions of rat liver cells. J. Agr. Food Chem. 21: 416-424, 1973.
 100. Lourteig, A., and C. E. Cardini. Action of lipases on some aromatic esters. Anales Farm Bioquim. Buenos Aires 18: 59-61, 1947.
 101. Lykken, L., and J. E. Casida. Metabolism of organic insecticide chemicals. Can. Med. Assoc. J. 100: 145-154, 1969.
 102. Main, A. R. The purification of the enzyme hydrolyzing diethyl p‐nitrophenyl phosphate (paraoxon) in sheep serum. Biochem. J. 74: 10-20, 1960.
 103. Main, A. R. Kinetics of active‐site‐directed irreversible inhibitions. In: Essays in Toxicology, edited by W. J. Hayes, Jr. New York: Academic Press, 1973, vol. 4, p. 59-105.
 104. Main, A. R., and P. E. Braid. Hydrolysis of malathion by aliesterase in vitro and in vivo. Biochem. J. 84: 255-263, 1962.
 105. Main, A. R., and W. C. Dauterman. Kinetics for the inhibition of carboxylesterase by malaoxon. Can. J. Biochem. 45: 757-771, 1967.
 106. March, R. B., T. R. Fukuto, R. L. Metcalf, and M. C. Maxon. Fate of P32 labeled malathion in the laying hen, white mouse and American cockroach. J. Econ. Entomol. 49: 185-195, 1956.
 107. Marton, A., and W. Kalow. Studies on aromatic esterase and cholinesterase of human serum. Can. J. Biochem. Physiol. 37: 1367-1373, 1959.
 108. Marton, A. V., and W. Kalow. Interaction between aromatic esterase of human serum and bivalent metal ions. Can. J. Biochem. Physiol. 40: 319-324, 1962.
 109. Matsumura, F., and A. W. A. Brown. Biochemistry of malathion resistance in Culex tarsalis. J. Econ. Entomol. 54: 1176-1185, 1961.
 110. Matsumura, F., and C. T. Ward. Degradation of insecticides by the human and rat liver. Arch. Environ. Health 13: 257-261, 1966.
 111. Mazur, A. An enzyme in animal tissues capable of hydrolyzing the phosphorus fluorine bond of alkyl fluorophosphates. J. Biol. Chem. 164: 271-289, 1946.
 112. Meagher, W. R. A heat labile insoluble conjugated form of 2,4‐dichlorophenoxyacetic acid and 2‐(2,4,5‐trichlorophenoxy)propionic acid in citrus peel. J. Agr. Food Chem. 14: 599-601, 1966.
 113. Melnikov, N. N. Chemistry of pesticides. In: Residue Reviews, edited by F. A. Gunther and J. D. Gunther. New York: Springer‐Verlag, 1971, vol. 36.
 114. Menzer, R. E., and W. C. Dauterman. Metabolism of some organophosphorus insecticides. J. Agr. Food Chem. 18: 1031-1037, 1970.
 115. Moore, D. J., and B. J. Rogers. The fate of long chain esters of 2,4‐D in plants. Weeds 8: 436-447, 1960.
 116. Mounter, L. A. Some studies of enzymatic effects of rabbit serum. J. Biol. Chem. 209: 813-817, 1954.
 117. Mounter, L. A. The complex nature of dialkylfluorophosphatases of hog and rat liver and kidney. J. Biol. Chem. 215: 705-711, 1955.
 118. Mounter, L. A. Metabolism of organophosphorus anticholinesterase agents. In: Handbuch der Experimentellen Pharmakologie, edited by O. Eichler and A. Farah. Berlin: Springer‐Verlag, 1963, vol. 15, p. 486-504.
 119. Mounter, L. A., H. C. Alexander, K. D. Tuck, and L. T. H. Dien. The pH dependence and dissociation constants of esterases and proteases treated with diisopropyl fluorophosphate. J. Biol. Chem. 226: 867-872, 1957.
 120. Mounter, L. A., R. F. Baxter, and A. Chanutin. Dialkylfluorophosphatases of microorganisms. J. Biol. Chem. 215: 699-704, 1955.
 121. Mounter, L. A., and A. Chanutin. Dialkylfluorophosphatase of kidney. II. Studies of activation and inhibition by metals. J. Biol. Chem. 204: 837-846, 1953.
 122. Mounter, L. A., and A. Chanutin. Dialkylfluorophosphatases of kidney. III. Studies of activation and inhibition by cofactors. J. Biol. Chem. 210: 219-226, 1954.
 123. Mounter, L. A., and L. T. H. Dien. Dialkylfluorophosphatases of kidney. V. The hydrolysis of organophosphorus compounds. J. Biol. Chem. 219: 685-690, 1956.
 124. Mounter, L. A., L. T. H. Dien, and A. Chanutin. The distribution of dialkylfluorophosphatases in the tissue of various species. J. Biol. Chem. 215: 691-697, 1955.
 125. Mounter, L. A., C. S. Floyd, and A. Chanutin. Dialkylfluorophosphatase of kidney. I. Purification and properties. J. Biol. Chem. 204: 221-232, 1953.
 126. Mounter, L. A., K. D. Tuck, H. C. Alexander, and L. T. H. Dien. The reactivity of esterases and proteases in the presence of organophosphorus compounds. J. Biol. Chem. 226: 873-879, 1957.
 127. Mounter, L. A., and V. P. Whittaker. The hydrolysis of esters of phenol by cholinesterases and other esterases. Biochem. J. 54: 551-559, 1953.
 128. Murphy, S. D. Liver metabolism and toxicity of thiophosphate insecticides in mammalian, avian and piscine species. Proc. Soc. Exptl. Biol. Med. 123: 392-398, 1966.
 129. Murphy, S. D. Malathion inhibition of esterases as a determinant of malathion toxicity. J. Pharmacol. Exptl. Therap. 156: 352-365, 1967.
 130. Murphy, S. D., R. L. Anderson, and K. P. Dubois. Potentiation of the toxicity of malathion by triorthotolylphosphate. Proc. Soc. Exptl. Biol. Med. 100: 483-487, 1959.
 131. Murphy, S. D., and K. L. Cheever. Feeding of insecticides Inhibition of carboxylesterase and cholinesterase activities in rats. Arch. Environ. Health 17: 249-758, 1968.
 132. Murphy, S. D., and K. P. DuBois. Quantitative measurement of inhibition of the enzyme detoxification of malathion by EPN (ethyl p‐nitrophenyl thiobenzenephosphonate). Proc. Soc. Exptl. Biol. Med. 96: 813-818, 1957.
 133. Myers, D. K. Competition of the aliesterase in rat serum with the pseudocholinesterase for diisopropyl fluorophosphate. Science 115: 568-570, 1952.
 134. Myers, D. K. Mechanism of the prophylactic action of diacetylmonoxime against sarin poisoning. Biochim. Biophys. Acta 34: 555-557, 1959.
 135. Myers, D. K., and A. Kemp. Inhibition of esterases by the fluorides of organic acids. Nature 173: 33-34, 1954.
 136. Neal, R. A., and K. P. DuBois. Studies on the mechanism of detoxification of cholinergic phosphorothioates. J. Pharmacol. Exptl. Therap. 148: 185-192, 1965.
 137. O'Brien, R. D. Properties and metabolism in the cockroach and mouse of malathion and malaoxon. J. Econ. Entomol. 50: 159-164, 1957.
 138. O'Brien, R. D. Toxic Phosphorus Esters. New York: Academic Press, 1960.
 139. O'Brien, R. D. Organophosphates and carbamates. In: Metabolic Inhibitors, edited by R. M. Hochster and J. H. Quastel. New York: Academic Press, 1963, vol. II, p. 207-241.
 140. O'Brien, R. D. Insecticides. Action and Metabolism. New York: Academic Press, 1967.
 141. O'Brien, R. D. Phosphorylation and carbamylation of cholinesterases. Ann. NY Acad. Sci. 160: 204-214, 1969.
 142. Plapp, F. W., W. S. Bigley, G. A. Chapman, and G. W. Eddy. Synergism of malathion against resistant houseflies and mosquitos. J. Econ. Entomol. 56: 643-649, 1963.
 143. Plapp, F. W., and G. W. Eddy. Synergism of malathion against resistant insects. Science 134: 2043-2044, 1961.
 144. Polak, R. L., and E. M. Cohen. The influence of triorthocresylphosphate on the distribution of 32P in the body of the rat after the injection of 32P‐sarin. Biochem. Pharmacol. 18: 813-820, 1969.
 145. Ramachandran, B. V., and G. Agren. Esterases of ratliver cell fractions. Correlation of DF32P‐binding capacity to esterase activity. Biochem. Pharmacol. 12: 981-988, 1963.
 146. Ramachandran, B. V., and G. Agren. Determination of DFPase in rabbit and rat tissues using DF32P. Biochem. Pharmacol. 13: 849-854, 1964.
 147. Reed, W. D., and T. R. Jukuto. The reactivation of carbamate‐inhibited cholinesterase, kinetic parameters. Pesticide Biochem. Physiol. 3: 120-130, 1973.
 148. Reiner, E. Spontaneous reactivation of phosphorylated and carbamylated cholinesterases. Bull. World Health Organ. 44: 109-112, 1971.
 149. Reiner, E., and W. N. Aldridge. Effect of pH on inhibition and spontaneous reactivation of acetylcholinesterase treated with esters of phosphorus acids and of carbamic acids. Biochem. J. 105: 171-179, 1967.
 150. Ryan, A. J. The metabolism of pesticidal carbamates. C.R.C. Critical Rev. Toxicol. 1: 33-54, 1971.
 151. Schaffer, C. B., C. P. Carpenter, and H. F. Smyth. Acute and subacute toxicity of di‐(2‐ethylhexyl)phthalate with note upon its metabolism. J. Ind. Hyg. Toxicol. 27: 130-135, 1945.
 152. Seume, F. W., and R. D. O'Brien. Potentiation of the toxicity to insects and mice of phosphorothionates containing carboxyester and carboxyamide groups. Toxicol. Appl. Pharmacol. 2: 495-503, 1960.
 153. Smith, C. C. Toxicity of butyl stearate, dibutyl sebacate dibutyl phthalate and methoxyethyl oleate. Arch. Ind. Hyg. Occupational Med. 7: 310-318, 1953.
 154. St. John, L. E., Jr., D. G. Wagner, and D. J. Lisk. Fate of atrazine, kuron, silvex and 2,4,5‐T in the dairy cow. J. Dairy Sci. 47: 1267-1270, 1964.
 155. Tove, S. B. The esterolytic activity of serum albumin. Biochim. Biophys. Acta 57: 230-235, 1962.
 156. Triolo, A. J., E. Mata, and J. M. Coon. Effects of organochlorine insecticides on the toxicity and in vitro plasma detoxication of paraoxon. Toxicol. Appl. Pharmacol. 17: 174-180, 1970.
 157. Uchida, T., W. C. Dauterman, and R. D. O'Brien. The metabolism of dimethoate by vertebrate tissue. J. Agr. Food Chem. 12: 48-52, 1964.
 158. Uchida, T., and R. D. O'Brien. Dimethoate degradation by human liver and its significance for acute toxicity. Toxicol. Appl. Pharmacol. 10: 89-94, 1967.
 159. Uchida, T., H. S. Rahmati, and R. D. O'Brien. The penetration and metabolism of H3‐dimethoate in insects. J. Econ. Entomol. 58: 831-835, 1965.
 160. Uchida, T., J. Zchintzsch, and R. D. O'Brien. Relation between synergism and metabolism of dimethoate in mammals and insects. Toxicol. Appl. Pharmacol. 8: 259-265, 1966.
 161. Welling, W., P. Blaakmeer, G. J. Vink, and S. Voerman. In vitro hydrolysis of paraoxon by parathion resistant houseflies. Pesticide Biochem. Physiol. 1: 61-70, 1973.
 162. Wheeler, L., and A. Strother. In vitro metabolism of the N‐methylcarbamates Zectran and Mesurol by liver, kidney, and blood of dogs and rats. J. Pharmacol. Exptl. Therap. 178: 371-382, 1971.
 163. Whitehouse, L. W., and D. J. Ecobichon. Paraoxon formation and hydrolysis by mammalian liver. Pesticide Biochem. Physiol. 5: 314-322, 1975.
 164. Wilde, C. E., and R. G. O. Kekwick. The arylesterases of human serum. Biochem. J. 91: 297-307, 1964.
 165. winteringham, F. P. W., A. Harrison, and P. M. Bridges. Absorption and metabolism of [14HC]pyrethroids by the adult housefly Musca domeestica L. in vivo. Biochem. J. 61: 359-367, 1955.
 166. Yamamoto, I., M. Elliott, and J. E. Casida. The metabolic fate of pyrethrin I, pyrethrin II and allethrin. Bull. World Health Organ. 44: 347-348, 1971.
 167. Yip, G., and J. W. Cook. Malathionase. III. Substrate specificity studies. J. Assoc. Offic. Agr. Chemists 42: 405-407, 1959.
 168. Zeller, E. A., G. A. Fleisher, R. A. McNaughton, and J. C. Schweppe. New substrates for cholinesterases. Proc. Soc. Exptl. Biol. Med. 71: 526-529, 1949.

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D. J. Ecobichon. Hydrolytic Transformation of Environmental Pollutants. Compr Physiol 2011, Supplement 26: Handbook of Physiology, Reactions to Environmental Agents: 441-454. First published in print 1977. doi: 10.1002/cphy.cp090127