FEBS LettersVolume 144, Issue 1 p. 43-46 Full-length articleFree Access Evidence for a change in catalytic properties of glyceraldehyde 3-phosphate dehydrogenase monomers upon their association in a tetramer L.I. Ashmarina, L.I. Ashmarina A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, Moscow, USSRSearch for more papers by this authorV.I. Muronetz, V.I. Muronetz A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, Moscow, USSRSearch for more papers by this authorN.K. Nagradova, N.K. Nagradova A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, Moscow, USSRSearch for more papers by this author L.I. Ashmarina, L.I. Ashmarina A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, Moscow, USSRSearch for more papers by this authorV.I. Muronetz, V.I. Muronetz A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, Moscow, USSRSearch for more papers by this authorN.K. Nagradova, N.K. Nagradova A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, Moscow, USSRSearch for more papers by this author First published: July 19, 1982 https://doi.org/10.1016/0014-5793(82)80565-6Citations: 8AboutPDF 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 References 1 L.I. Ashmarina, V.I. Muronetz, N.K. Nagradova, Biochem. Int., 1, (1980), 47– 54. 2 V.I. Muronetz, V.S. Zueva, N.K. Nagradova, FEBS Lett., 107, (1979), 277– 280. 3 L.I. Ashmarina, V.I. Muronetz, N.K. Nagradova, FEBS Lett., 128, (1981), 22– 26. 4 W.B. Stallcup, D.E. Koshland jr, Biochem. Biophys. Res. Commun., 49, (1972), 1108– 1114. 5 B.A. Cook, D.E. Koshland jr, Biochemistry, 9, (1970), 3337– 3342. 6 L.I. Ashmarina, V.I. Muronetz, N.K. Nagradova, Biochem. Int., 3, (1981), 415– 424. 7 T.O. Golovina, T.V. Cherednikova, A.I. Mevkh, N.K. Nagradova, Analyt. Biochem., 83, (1977), 778– 781. 8 A. Szewezuk, E. Wolna, M. Wolny, T. Baranowski, Acta Biochim. Pol., 8, (1961), 201– 207. 9 E. Negelein, H. Brömel, Biochem. Z., 303, (1939), 132– 144. 10 C.S. Furfine, S.F. Velick, J. Biol. Chem., 240, (1965), 844– 855. 11 R.G. Duggleby, D.T. Dennis, J. Biol. Chem., 249, (1974), 175– 181. 12 O.P. Malhotra, S.A. Bernhard, F. Seydoux, Biochimie, 63, (1981), 131– 141. 13 N. Kellershohn, F.J. Seydoux, Biochemistry, 18, (1979), 2465– 2470. 14 B. Schwendimann, D. Ingbar, S.A. Bernhard, J. Mol. Biol., 108, (1976), 123– 138. 15 J.J.M. De Vijlder, A.G. Hilvers, J.M.J. Van Lis, E.C. Slater, Biochim. Biophys. Acta, 191, (1969), 221– 228. Citing Literature Volume144, Issue1July 19, 1982Pages 43-46 ReferencesRelatedInformation