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Kinetic isotope effects in the NAD‐ and NADP‐specific isocitrate dehydrogenases of pig heart

1974; Wiley; Volume: 49; Issue: 1 Linguagem: Inglês

10.1016/0014-5793(74)80648-4

1873-3468

N. Ramachandran, Marciana Durbano, Roberta F. Colman,

Metabolism and Genetic Disorders

FEBS LettersVolume 49, Issue 1 p. 129-133 Full-length articleFree Access Kinetic isotope effects in the NAD- and NADP-specific isocitrate dehydrogenases of pig heart N. Ramachandran, N. Ramachandran Department of Chemistry, University of Delaware, Newark, Delaware, 19711, USASearch for more papers by this authorMarciana Durbano, Marciana Durbano Department of Chemistry, University of Delaware, Newark, Delaware, 19711, USASearch for more papers by this authorRoberta F. Colman, Roberta F. Colman Department of Chemistry, University of Delaware, Newark, Delaware, 19711, USASearch for more papers by this author N. Ramachandran, N. Ramachandran Department of Chemistry, University of Delaware, Newark, Delaware, 19711, USASearch for more papers by this authorMarciana Durbano, Marciana Durbano Department of Chemistry, University of Delaware, Newark, Delaware, 19711, USASearch for more papers by this authorRoberta F. Colman, Roberta F. Colman Department of Chemistry, University of Delaware, Newark, Delaware, 19711, USASearch for more papers by this author First published: December 01, 1974 https://doi.org/10.1016/0014-5793(74)80648-4Citations: 13AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References 1 G.W.E. Plaut, P.D. Boyer H. Lardy K. Myrback The Enzyme 7, (1963), 105– 126. 2nd Edn. 2 R.F. Chen, G.W.E. Plaut, Biochem., 2, (1963), 752– 756. 3 G.E. Lienhard, I.A. Rose, Biochem., 3, (1964), 185– 190. 4 S. Englard, I. Listowsky, Biochem, 3, (1963), 185– 190. 5 Z.B. Rose, J. Biol. Chem., 241, (1966), 2311– 2313. 6 R.F. Colman, R.C. Szeto, P. Cohen, Biochem., 9, (1970), 4945– 4949. 7 P.F. Cohen, R.F. Colman, Biochem. Biophys. Acta, 242, (1971), 325– 330. 8 W.C. Shen, L. Mauck, R.F. Colman, J. Biol. Chem., 249, (1974), in press 9 G.W.E. Plaut, Current Topics in Cellular Regulation, 2, (1970), 1– 27. 10 R.F. Colman, R. Chu, Biochem. Biophys. Res. Commun., 34, (1969), 528– 535. 11 M.H. O'Leary, Biochem. Biophys. Acta, 235, (1971), 14– 18. 12 M.L. Bender, E.J. Pollack, M. Neveu, J. Am. Chem. Soc., 84, (1962), 595– 599. 13 M.L. Bender, G.R. Schonbaum, G.A. Hamilton, B. Zerner, J. Am. Chem. Soc., 83, (1961), 1255– 1256. 14 R.F. Colman, J. Biol. Chem., 243, (1968), 2454– 2464. 15 S. Ochoa, J. Biol. Chem., 174, (1948), 115– 122. 16 N.G. Gaylord, Reduction with Complex Metal Hydrides (1956), Interscience N.Y 17– 17 R.E. Davis, E. Bromels, C.L. Kibby, J. Am. Chem. Soc., 84, (1962), 885– 892. 18 K. LaNoue, W.J. Micklas, J.R. Williamson, J. Biol. Chem., 245, (1970), 102– 111. 19 J.J. Villafranca, R.F. Colman, Biochem., 13, (1974), 1152– 1160. 20 P.K. Glasoe, F.A. Long, J. Phys. Chem., 64, (1960), 188– 190. 21 P.A. Srere, G.W. Kosicki, R. Lumry, Biochem. Biophys. Acta, 50, (1961), 184– 185. 22 P. Cohen, R.F. Colman, Biochemistry, 11, (1972), 1501– 1508. 23 J.H. Richards, P.D. Boyer The Enzymes 2, (1970), 324– 3rd Edn. 24 W.P. Jencks, Catalysis in Chemistry and Enzymology (1969), McGraw-Hill N.Y 219– W.P. Jencks, Catalysis in Chemistry and Enzymology (1969), McGraw-Hill N.Y 274– 281. 25 S.W. Englander, N.W. Downer, H. Teitelbaum, Ann. Rev. Biochem., 41, (1972), 903– 924. Citing Literature Volume49, Issue1December 01, 1974Pages 129-133 ReferencesRelatedInformation