Studies of Glutamate Dehydrogenase. The Binding of NADH and NADPH to Beef-Liver Glutamate Dehydrogenase
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Kinetic studies of dogfish liver glutamate dehydrogenase.
Initial-rate studies were made of the oxidation of L-glutamate by NAD+ and NADP+ catalysed by highly purified preparations of dogfish liver glutamate dehydrogenase. With NAD+ as coenzyme the kinetics show the same features of coenzyme activation as seen with the bovine liver enzyme [Engel & Dalziel (1969) Biochem. J. 115, 621--631]. With NADP+ as coenzyme, initial rates are much slower than wit...
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NAD+ with a nitroxide piperidine ring linked to the NH2 group of the adenine possesses full coenzymatic activity with glutamate dehydrogenase. Electron spin resonance spectra in the presence of glutamate dehydrogenase show mixtures of free and strongly immobilized spin-label. Binding studies in phosphate buffer demonstrate: (a) weak binary binding to the enzyme with a dissociation constant in t...
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published by admin on Fri, 03/14/2014 8:53am Title Beef liver L-Glutamate dehydrogenase mechanism: presteady state study of the catalytic reduction of 2.oxoglutarate by NADPH. Publication Type Journal Article Year of Publication 1975 Authors Jallon, JM, Risler, Y, Iwatsubo, M Journal Biochem Biophys Res Commun Volume 67 Issue 4 Pagination 1527-36 Date Published 1975 Dec 15 ISSN 0006-291X
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1974
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1974.tb03301.x