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Studies of Glutamate Dehydrogenase.
- Source :
-
European Journal of Biochemistry . Dec73 Part 1, Vol. 40 Issue 1, p543-548. 6p. - Publication Year :
- 1973
-
Abstract
- Specific interaction between α-NADH and glutamate dehydrogenase is demonstrated by difference spectroscopy, circular dichroism and fluorescence measurements. Quantitative binding studies in the preparative ultracentrifuge yield six identical α-NADH binding sites per oligomer with a dissociation constant of 20 μM. Evidence for six to eight additional, very weak α-NADH binding sites is presented. Excess ADP prevents the binding of α-NADH to the tight binding sites, indicating competition of the two nucleotides. In the enzymatic reaction, α-NADH is inactive as a coenzyme; however, like ADP, it is an activator of the reductive amination reaction of 2-oxoglutarate. α-NADH reduces the self-inhibition of high β-NADH concentrations and thus again parallels the effects caused by ADP. Contrary to β-NADH or β-NADH plus GTP, α-NADH or α-NADH plus GTP does not affect the dissociation-association equilibrium of glutamate dehydrogenase. The results are consistent with the assumption of six binding sites for α-NADH, which are identical with the ADP binding sites and most probably the six non-active β-NADH binding sites. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 40
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 13669599
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1973.tb03225.x