Bovine Glutamate Dehydrogenase
نویسندگان
چکیده
منابع مشابه
Regulation of Bovine Glutamate Dehydrogenase
The activity of bovine liver glutamate dehydrogenase is affected in several ways depending on substrate concentrations and pH. At pH 6.5 and below, both oxidative deamination and reductive amination reactions are inhibited by ADP. At pH 7.0 and above both activatory and inhibitory effects can be observed depending on substrate concentrations. The effects are explicable in terms of a model with ...
متن کاملDual nucleotide specificity of bovine glutamate dehydrogenase
The thionicotinamide analogues of NAD+ and NADP+ were shown to be good alternative coenzymes for bovine glutamate dehydrogenase, with similar affinity and approx. 40% of the maximum velocity obtained with the natural coenzymes. Both thionicotinamide analogues show non-linear Lineweaver-Burk plots, which with the natural coenzymes have been attributed to negative co-operativity. Since the reduce...
متن کاملInactivation of bovine glutamate dehydrogenase by carbamyl phosphate and cyanate.
By kinetic studies and the identification of the labeled peptide of the [WIKNCO-modified protein, the inactivation of bovine liver glutamate dehydrogenase by potassium cyanate can be attributed to the carbamylation of the e-amino group of lysine-97. Although the e-amino group of lysine-97 is the major site of carbamylation by cyanate, the oc-amino group of alanine-l and E-amino group of lysine-...
متن کاملThe Interaction of Tetraiodofluorescein with Glutamate Dehydrogenase from Bovine Liver
Reports from various laboratories have dealt with the binding properties of glutamate dehydrogenase from bovine liver (EC 1.4.1.3) (Pantaloni & Dessen, 1969; Huang & Frieden, 1969; Malcolm, 1972; Brown et al., 1973; Koberstein & Sund, 1973), but unfortunately these reports differ considerably over the number and nature of glutamate dehydrogenase coenzyme-binding sites as well as the magnitude o...
متن کاملA product-inhibition study of bovine liver glutamate dehydrogenase.
1. Initial rates of oxidative deamination of L-glutamate with NAD+ as coenzyme, and of reductive aminiation of 2-oxoglutarate with NADH as coenzyme, catalysed by bovine liver glutamate dehydrogenase were measured in 0.111 M-sodium phosphate buffer, pH 7, at 25 degrees C, in the absence and presence of product inhibitors. All 12 possible combinations of variable substrate and product inhibitor w...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1973
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)44012-x