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Effect of Inorganic Fluoride on Enzymes

Wiseman, Alan·1970·Pharmacology of Fluorides
DOI 10.1007/978-3-642-99973-4_2
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  1. Adams, E., Smith, E.L.: Peptidases of erythrocytes. II. Isolation and properties of prolidase. J. biol. Chem. 198, 671—682 (1952) · DOI
  2. Agner, K., Theorell, H.: On the mechanism of the catalase inhibition by anions. Arch. Bio-chem. Biophys. 10, 321—338 (1946)
  3. Ahrens, G., Bramstedt, F.: Action of low fluoride concentrations on salivary phosphatases. CRCA Commun. Congr. Organ. Europeen. Coord. Reeh. Fluor Prophilaxie Carie Dentaire, 6th, Pavia, Italy, 1959, 229—236 (Pub. 1962); cf. Chem. Abstr. 58, 9376 (1963)
  4. Axelrod, B., Bandtjrski, R.S.: Phosphoglyeerate kinase in higher plants. J. biol. Chem. 204, 939—948 (1953)
  5. Barkttlis, S.S., Lehninger, A.L.: Myokinase and the adenine nucleotide specificity in oxidative phosphorylation. J. biol. Chem. 190, 339—359 (1951)
  6. Belfanti, S., Contardia, A., Ercoli, A.: XCIX. Researches on the phosphatases. II. In-activation and reactivation of the phosphatases of animal organs. Biochem. J. 29, 842—846 (1935) · DOI
  7. Beltz, R.E.: Comparison of the content of thymidylate synthetase, deoxycytidylate deaminase and deoxyribonuclease kinases in normal and regenerating rat liver. Arch. Biochem. Biophys. 99, 304—312 (1962) · DOI
  8. Borei, H.: Inhibition of cellular oxidation by fluoride. Arkiv Kemi, Mineral. Geol. 20 A (No. 8), 1—125 (1945)
  9. Borst, P.: Pathways of glutamate oxidation by mitochondria isolated from different tissues. Biochim. Biophys. Acta 57, 256—269 (1962)
  10. Boser, H.: Selective reactivation of an enolase reaction by zinc ions after inhibition by fluorides. Naturwissenschaften 44, 586 (1957) · DOI
  11. Bray, R.C.: Xanthine oxidase. In: P.D. Boyer, H. Lardy, and K. Myrback, Eds., The Enzymes, Vol. VII, pp. 533—556. New York: Academic Press 1963
  12. Bucher, T.: Enolase from brewer yeast. In: S.P. Colo wick, and N. O. Kaplan, Eds., Methods in Enzymology, Vol. I, pp. 427—435. New York: Academic Press 1955
  13. Btjrstone, M. S.: Esterase activity of developing bones and teeth. Arch. Pathol. 63, 164—167 (1957)
  14. Callaghan, O.K., Weber, G.: Kinetic studies on rabbit muscle myokinase. Biochem. J. 73, 473—485 (1959) · DOI
  15. Cantoni, G.L.: Methionine-activating enzyme, liver. In: S.P. Colowick, and N.O. Kaplan Eds., Methods in Enzymology, Vol. II, pp. 254—256. New York: Academic Press 1955
  16. Chance, B.: The effect of pH upon the equilibria of catalase compounds. J. biol. Chem. 194, 483—496 (1952)
  17. Chaudhary, K.D., Moorjani, S., Lemonde, A.: Kinetic studies on acid phosphatase in Tri-bolium confusum Duval. Canad. J. Biochem. 42, 1769—1775 (1964)
  18. Cemasoni, C: Inhibition of cholinesterases by F’ in vitro. Biochem. J. 99,133—137 (1966)
  19. Cowgill, R. W., Pizer, L.I.: Purification and some properties of phosphoglyeerie acid mutase from rabbit skeletal muscle. J. biol. Chem. 223, 885—895 (1956) · DOI
  20. Denes, G.: Studies on the enzymatic synthesis of acid amide and peptide linkages. II. The mechanism of fluoride inhibition of glutamine synthesis and the prosthetic group of the enzyme. Acta physiol. Acad. Sci. hung. 6, 201—208 (1954); cf. Chem. Abstr. 49, 8337 (1955)
  21. Dixon, M., Webb, E.C.: Enzymes. 2nd ed. London: Longmans 1964
  22. Dondoroff, M.: Disaccharide phosphorylases. In: P.D. Boyer, H. Lardy, and K. Myrback, Eds., The Enzymes, Vol. V, pp. 229—236. New York: Academic Press 1959
  23. Dybing, O., Loe, L.V.: Fluoride poisoning and cholinesterase in rats. Acta Pharmacol. Toxicol. 12, 364—368 (1956)
  24. Ebata, M., Sato, R., Bak, T.: The enzymic phosphorylation of sedoheptulose. J. Biochem. (Tokyo) 42, 715—725 (1955) · DOI
  25. Elliott, W. H.: Effect of fluoride on enzymic synthesis of glutamine by sheep-brain extract. Studies on the enzymic synthesis of glutamine. Biochem. J. 49, 106—112 (1951) · DOI
  26. Elliott, W. H.: Isolation of glutamine synthetase and glutamotransferase from green peas. J. biol. Chem. 201, 661—672 (1953) · DOI
  27. Elliott, W. H.: The breakdown of ATP accompanying cholic acid activation by guinea-pig liver microsomes. Biochem. J. 65, 315—321 (1957)
  28. Ennor, A. A., Rosenberg, BL: Some properties of creative phosphokinase. Biochem. J. 57, 203—212 (1954) · DOI
  29. Plaks, J.G.: 5’-Phosphoribose pyrophosphokinase. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. VI, pp. 158—162. New York: Academic Press 1963
  30. Pridovioh, I.: Inhibition of acetoacetic decarboxylase by anions. The Hofmeister lyotropic series. J. biol. Chem. 238, 592—598 (1963)
  31. George, B.: The chemical nature of the second hydrogen peroxide compound formed by cytochrome c peroxidase and horseradish peroxidase. II. Formation and decomposition. Biochem. J. 55, 220—230 (1953)
  32. Gore, M.B.R.: Adenosine triphosphatase activity of brain. Biochem. J. 50, 18—24 (1952)
  33. Grunberg-Manago, M., Oritz, P. J., Ochoa, S.: Enzymic synthesis of polynucleotides. I. Polynucleotide phosphorylase of Azotobacter vinelandii. Biochim. Biophys. Acta 20, 269—285 (1956) · DOI
  34. Gunsalus, I.C., Razzell, W.E.: Pyridoxal kinase from brewer’s yeast. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. II, pp. 646—649. New York: Academic Press 1955
  35. Harris, H., Whittaker, M.: Differential inhibition of “usual” and “atypical” serum cholinesterase by NaCl and NaF. Ann. Human Genet. 27, 53—58 (1963—1964)
  36. Hayaishi, O.: Phospholipases. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. I, pp. 660—672. New York: Academic Press 1955
  37. Hayaishi, O.: A bacterial pterin deaminase. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. VI, pp. 359—363. New York: Academic Press 1963
  38. Heppel, L.A., Hilmoe, R. J.: Purification and properties of 5’-nucleotidase. J. biol. Chem. 188, 665—676 (1951) · DOI
  39. Hewitt, E. J., Nicholas, J.D.: Cations and anions. In: R.M. Hochester and J.H. Quastel, Eds., Metabolic Inhibitors, Vol. II, pp. 311—436. New York: Academic Press 1963
  40. Hoestee, B.H. J.: Inhibition of horse liver esterases by fluoride. J. biol. Chem. 207, 211—218 (1954)
  41. Jones, M.E.: Carbamyl phosphate synthesis and utilization. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. V, pp. 903—925. New York: Academic Press 1962
  42. Juni, E.: Acetoin formation in bacteria. In: S. O. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. I, pp. 471—475. New York: Academic Press 1955
  43. Kaufman, S.: a-Ketoglutaric dehydrogenase system and phosphorylating enzyme from heart muscle. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. I, pp. 714—722. New York: Academic Press 1955
  44. Kielley, W.W.: Magnesium-activated muscle ATP-ases. In: S.P. Colowick, and N.O. Kaplan, Eds., Methods in Enzymology, Vol. II, pp. 588—591. New York: Academic Press 1955
  45. Kirkland, R.J. A., Turner, J.F.: Nucleoside diphosphokinase of pea seeds. Biochem. J. 72, 716—720 (1959)
  46. Kornberg, A., Lieberman, I., Sims, E.S.: Enzymic synthesis of purine nucleotides. J. biol. Chem. 215, 417—427 (1955)
  47. Kornberg, S.R.: Metaphosphate synthesis by an enzyme from E. coli. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. VI, pp. 262—265. New York: Academic Press 1963
  48. Kurahashi, K., Sugimura, A.: Purification and properties of galactose 1-phosphate uridyl transferase from Escherichia coli. J. biol. Chem. 235, 940—946 (1960) · DOI
  49. Lee, Y.: 5’-Adenylic acid deaminase. II. Properties and kinetic studies. J. biol. Chem. 227, 999—1007 (1957)
  50. Lehman, I.R.: DNA synthesis (bacterial). In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. VI, pp. 34—39. New York: Academic Press 1963
  51. Leloir, L.E., Trucco, R.E., Cardini, C.E., Paladini, A.C, Caputto, R.: The formation of glucose diphosphate by E. coli. Arch. Biochem. Biophys. 24, 65—74 (1949)
  52. Lerner, A. B.: Mammalian tyrosinase: effect of ions on enzyme action. Arch. Biochem. Biophys. 36, 473–481 (1952) · DOI
  53. Leuthabdt, E., Bbuttin, A.: Concerning the myokinase of liver. Helv. Chim. Acta 35, 464––467 (1952) · DOI
  54. Ling, K.H., Marcus, F., Labdy, H.A.: Purification and some properties of rabbit skeletal muscle phosphofructokinase. J. biol. Chem. 240, 1893—1899 (1965)
  55. Little, H.N.: Nitroethane oxidase. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. II, pp. 400—402. New York: Academic Press 1955
  56. London, M., McHugh, R., Hudson, P.B.: Thermal stabilization of prostatic acid phosphatase by fluoride. Arch. Biochem. Biophys. 55, 121—125 (1955) · DOI
  57. Maehly, A.C.: Myeloperoxidase. In: S.P. Colowiok and N.O. Kaplan, Eds., Methods in Enzymology, Vol. II, pp. 794—801. New York: Academic Press 1955
  58. Malsteom, B.G., Labsson-Raznikiewicz, M.: 3-Phosphoglycerate kinase. In: P.D. Boyeb, H. Labdy, and K. Mybback, Eds., The Enzymes, Vol. VI, pp. 85—94. New York: Academic Press 1963
  59. Mandl, I., Neubebg, C: Metaphosphatases. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. II, pp. 577—580. New York: Academic Press 1955
  60. Massey, V.: The role of iron in beef-heart succinic dehydrogenase. Biochim. Biophys. Acta 30, 500—509 (1958)
  61. Mathies, J. C.: Preparation and properties of highly purified phosphatase from swine kidneys. J. biol. Chem. 233, 1121—1127 (1958) · DOI
  62. Mazelis, M.: Particulate adenylic kinase in higher plants. Plant Physiol. 31, 37—43 (1956) · DOI
  63. McDonald, M.R.: Deoxyribonucleases. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. II, pp. 437—447. New York: Academic Press 1955
  64. McGaughey, C, Stowell, E.C.: Estimation of a few nanograms of fluoride in presence of phosphate by use of liver esterase. Anal. Chem. 36, 2344—2350 (1964) · DOI
  65. Meyebs, D.K., Slatee, E.C.: Effect of fluoride on enzymic hydrolysis of ATP by liver mitochondria. Biochem. J. 65, 572—579 (1957)
  66. Naganna, B., Menon, V.K.N.: Erythrocyte pyrophosphatase in health and disease. I. Properties of the enzyme. J. biol. Chem. 174, 501—522 (1948) · DOI
  67. Naganna, B., Raman, A., Venugopal, B., Sbipathi, C.E.: Potato pyrophosphatases. Biochem. J. 60, 215—233 (1955)
  68. Najjar, V.A.: The isolation and properties of phosphoglucomutase. J. biol. Chem. 175, 281—290 (1948) · DOI
  69. Najjar, V.A.: The role of 22 metal ions in enzyme systems. In: W.D. McElboy and B. Glass, Eds., Phosphorus Metabolism, Vol. I, pp. 500—520. Baltimore: Johns Hopkins Press 1951
  70. Najjar, V.A.: Phosphoglucomutase. In: P.D. Boyeb, H. Labdy, and K. Mybback, Eds., The Enzymes, Vol. VI, pp. 161—178. New York: Academic Press 1963
  71. Nandy, M., Ganguli, N.C.: Synthesis of 5-dehydroshikimic acid from carbohydrates by mung bean seedling extract. J. Sci. Ind. Res. (India) 21C, 34—38 (1962); cf. Chem. Abstr. 57, 14164 (1962)
  72. Nabayanaswami, A.: Creative phosphokinase in mammalian brain. Biochem. J. 52, 295—301 (1952)
  73. Nicholls, P.: The action of anions on catalase peroxide compounds. Biochem. J. 81, 365—374 (1961)
  74. Nikiforuk, G., Colowick, S.P.: 5’-AMP deaminase from muscle. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. II, pp. 469—473. New York: Academic Press 1955
  75. Nikiforuk, G.: The purification and properties of S-adenylic acid deaminase from muscle. J. biol. Chem. 219, 119—129 (1956) · DOI
  76. Noda, L.: Nucleoside triphosphate-nucleoside monophosphokinases. In: P.D. Boyeb, H. Labdy and K. Mybback, Eds., The Enzymes, Vol. VI, pp. 139—149. New York: Academic Press 1963
  77. Nobdlie, R., Labdy, BL: Phosphonyl group transfer. In: P.D. Boyeb, H. Labdy, and K. Mybback, Eds., The Enzymes, Vol. VI, pp. 4—46. New York: Academic Press 1963
  78. Oginsky, E.L.: Arginine dihydrolase. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. II, pp. 374—378. New York: Academic Press 1955
  79. Oginsky, E.L., Gehbig, R.F.: The arginase dihydrolase system of S. faecalis. II. The decomposition of citrulline. J. biol. Chem. 204, 721—729 (1953) · DOI
  80. Petebs, R.A.: Lethal synthesis. Proc. roy. Soc. B 139, 143—170 (1952)
  81. Petebs, R.A., Shobthouse, M., Mubeay, L.R.: Enolase and fluorophosphate. Nature (Lond.) 202, 1331—1332 (1964)
  82. Pizer, C.I.: Phosphoglycerate mutase. In: P.D. Boyeb, H. Labdy and K. Mybback, Eds., The Enzymes, Vol. VI, pp. 179—192. New York: Academic Press 1963
  83. Plane, R.A., Theobell, H.: Liver alcohol dehydrogenase. IV. Kinetics in the presence of zine binding agents. Acta Chem. Scand. 15, 1866—1874 (1961) · DOI
  84. Plattt, G. W.E.: Inosine diphosphatase (nucleoside diphosphatase) from mammalian liver. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. VI, pp. 231—236. New York:Academic Press 1963
  85. Rackeb, E.: Sedoheptulose-1,7-diphosphatase from yeast. In: S. P. Colowick and N. O. Kaplan, Eds., Methods in Enzymology, Vol. V, pp. 270—272. New York: Academic Press 1962a
  86. Rackeb, E.: Fructose 1,6-diphosphatase from spinach leaves. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. V, pp. 272—276. New York: Academic Press 1962b
  87. Rall, T.W., Sutherland, E.W.: Enzymes concerned with interconversion of liver phosphor-rylases. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. V, pp. 377—391. New York: Academic Press 1962
  88. Ratner, S.: Urea synthesis and metabolism of arginine and citrulline. In: F.F. Nord, Ed., Advances in Enzymology, Vol. 15, pp. 319—387. New York: Academic Press 1954
  89. Ratner, S.: Enzymic synthesis of arginine (condensing and splitting of enzymes). In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. II, pp. 356—367. New York: Academic Press 1955
  90. Ratner, S.: N-Transfer from aspartic acid in the formation of amide, amidine and guanidino groups. In: P.D. Boyer, H. Lardy, and K. Myrback, Eds., The Enzymes, Vol. VI, pp. 496—513. New York: Academic Press 1963
  91. Ratner, S., Petrack, B.: Biosynthesis of urea. III. Further studies on arginine synthesis from citrulline. J. biol. Chem. 191, 693—705 (1951) · DOI
  92. Ratner, S., Biosynthesis of urea. IV. Further studies on condensation in arginine synthesis from citrulline. J. biol. Chem. 200, 161—185 (1953)
  93. Ravel, J.M., Mosteller, R.D., Hardesty, B.: NaF inhibition of the initial binding of aminoacyl-sRNA to reticulocyte ribosomes. Proc. Natl. Acad. Sci. U.S. 56, 701—708 (1966) · DOI
  94. Reiner, J.M., Tstjbol, K.K., Hudson, P.B.: Acid phosphatase. IV. Fluoride inhibition of prostatic acid phosphatase. Arch. Biochem. Biophys. 56, 165—183 (1955) · DOI
  95. Revel, H.P.: Phosphoprotein phosphatase. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. VI, pp. 211—214. New York: Academic Press 1963
  96. Roberts, D. W. A.: The wheat leaf phosphatases. V. Some properties of the enzymic system hydrolyzing β-glycerophosphate in crude juice preparations. Canad. J. Biochem. Physiol. 41, 113—120 (1963)
  97. Roche, J., Thoai, N. V.: Phosphatase alcaline. Advances in Enzymology, Vol. 10, pp. 83—122. New York: Academic Press 1950
  98. Schramm, M.: O-Phosphoserine phosphatase. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology Vol. VI, pp. 215—218. New York: Academic Press 1963
  99. Siekevitz, P., Potter, V.R.: The adenylate kinase of rat liver mitochondria. J. biol. Chem. 200, 187—196 (1953) · DOI
  100. Slade, H. D.: The effect of fluoride on the arsenolysis of citrulline by soluble enzymes of streptococci. Biochim. Biophys. Acta 15, 411—414 (1954) · DOI
  101. Slater, E. C.: Mechanism of inhibition of succinic dehydrogenase by fluoride and phosphate. Biochem. J. 58, i—ii (1954) · DOI
  102. Slater, E. C., Bonner, W. D.: The effect of fluoride on the succinic oxidase system. Biochem. J. 52, 185—196 (1952) · DOI
  103. Smith, Q.T., Armstrong, W.D., Singer, L.: Inhibition of human salivary and prostatic acid phosphatase and yeast enolase by low fluoride concentrations. Proc. Soc. exp. Biol. Med. 102, 170—173 (1959)
  104. Somorgyi, J., Vineze, I.: Mitochondrial and extramitochondrial ATPases in brain tissue. II. Some properties of extramitochondrial ATPases. Acta physiol. Acad. Sci. hung. 21, 29—41 (1962)
  105. Speck, J.F.: The enzymatic synthesis of glutamine. A reaction utilizing ATP. J. biol. Chem. 179, 1405—1426 (1949)
  106. Stekol, J.A.: Newer methods for preparation of S-adenosylmethionine and derivatives. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. VI, pp. 566—577. New York: Academic Press 1963
  107. Stoppant, A., Brignone, J. A.: Protection of succinic dehydrogenase thiol groups by fluoride and phosphate. Biochem. J. 64, 196—200 (1956)
  108. Stumpp, P.K.: y-Glutamyltransferase (plants). In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. II, pp. 263—267. New York: Academic Press 1955
  109. Sund, H., Theorell, H.: Alcohol dehydrogenase. In: P.D. Boyer, H. Lardy and K. Myrback, Eds., The Enzymes, Vol. VII, pp. 25—83. New York: Academic Press 1963
  110. Suztje, G.: The enzymic synthesis of bacterial phytoene from mevalonic aeid-2-14C. J. Biochem. (Tokyo) 51, 246—252 (1962)
  111. Takahashi, H., Taniguchi, S., Egami, P.: Inorganic nitrogen compounds: Distribution and metabolism. In: M. Florkin and H.S. Mason, Eds., Comparative Biochemistry, Vol. 5, pp. 91—202. New York: Academic Press 1963
  112. Tietz, A., Oohoa, S.: Pluorokinase and pyruvic kinase. Arch. Biochem. Biophys. 78, 477—493 (1958) · DOI
  113. Toida, I.: Hydrazidase. II. Inhibition by fluoride. J. Biochem. (Tokyo) 53, 18—22 (1963) · DOI
  114. Umbreit, W.W., Btjrris, R.H., Stattffer, J.P.: Manometric Techniques, pp. 112—113. Minneapolis, Minnesota: Burgess Publishing Company 1964
  115. Vintjela, E., Salas, M.L., Salas, M., Sols, A.: Two interconvertible forms of yeast phospho-fructokinase with different sensitivity to endproduct inhibition. Biochem. biophys. Res. Commun. 15, 243—249 (1964)
  116. Waelsch, H., Mycek, M. J.: Transglutaminase. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. V, pp. 833—838. New York: Academic Press 1962
  117. Warburg, O., Christian, W.: Chemical mechanism of fluoride inhibition of yeast. Natur-wissenschaften 29, 590 (1941a) · DOI
  118. Warburg, O., Christian, W.: Chemical mechanism of fluoride inhibition of yeast. Naturwissenschaften 29,590 (1941b) · DOI
  119. Warburg, O., Christian, W.: Isolation and crystallization of enolase. Biochem. Z. 310, 384—421 (1942). cf. Chem. Abstr. 36, 4141 (1942)
  120. Webb, J.L.: Enzyme and Metabolic Inhibitors, Vol. I, p. 251. New York: Academic Press 1963a · DOI
  121. Webb, J.L.: Enzyme and Metabolic Inhibitors, Vol. I, pp. 13—48. New York: Academic Press 1963b · DOI
  122. Webb, J.L.: Enzyme and Metabolic Inhibitors, Vol. I, p. 492. New York: Academic Press 1963c · DOI
  123. Whelan, W.J.: Phosphorylases from plants. In: S.P. Colowick and N.O. Kaplan, Eds., Methods in Enzymology, Vol. I, 192—200. New York: Academic Press 1955
  124. Whittaker, J.R., Tappel, A. L.: Modification of enzymic activity. II. Effects of salts on a-amylase, alcohol dehydrogenase and hematin catalysis. Biochim. Biophys. Acta 62, 310—317 (1962)
  125. Wildman, S. G., Bonner, J.: The proteins of green leaves. I. Isolation, enzymatic properties and auxin content of spinach cytoplasmic proteins. Arch. Biochem. Biophys. 14, 381—413 (1947)
  126. Zimmerman, S.B.: Deoxy CTP and deoxy CDP-splitting enzyme. In: S.P. Colowick, and N.O. Kaplan, Eds., Methods in Enzymology, Vol. VI, pp. 258—263. New York: Academic Press 1963

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Authors
Wiseman, A.
Venue
Pharmacology of Fluorides
Publisher
Springer Berlin Heidelberg
Published
1970
Pages
48-97
DOI
10.1007/978-3-642-99973-4_2
Cited by
24
References
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