Liver bovine, glutamate dehydrogenase

Bovine Liver Glutamate Dehydrogenase Henryk Eisenberg, Robert Josephs, and Emil Reisler... 

Figure 2. SDS gel electrophoresis of the products of partial cystine cleavage for several test proteins. A. molecular weight standards, B. yeast alcohol dehydrogenase. C. P-lactoglobulin, D. hen egg lysozyme, E. ovalbumin, F. calf fetal serum fetuin. Molecular weight standards are indicated by arrows on the left side of the gel and are bovine serum albumin (66,300), bovine liver glutamate dehydrogenase (55,400), porcine muscle lactate ddiydiogenase (36,500), bovine erythrocyte carbonic anhydrase (31,000), soybean trypsin inhibitor (21,500), hen egg lysozyme (14,400), bovine lung aprotinin (6,000), unresolved bovine pancreatic insulin A and B chains.

Chen, S.S., and Engel, PC. (1975) The equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal5 -phosphate. A demonstration that covalent modification with this reagent completely abolishes catalytic activity. Biochem. J. 147, 351-358. 

Substrate inhibition of bovine liver glutamate dehydrogenase has not been studied in such detail. It is most marked when the NAD(P) concentration is also large (11), and is relieved by ADP. This appears to be the reason why ADP activates the enzyme when large glutamate and... 

In many cases, 5 -FSBA reacts at active sites however, in bovine liver glutamate dehydrogenase, all the fluorosulfonylbenzoyl nucleosides react at regulatory sites. This enzyme is a hexamer of identical subunits, each of which has two regulatory sites for ADP, two for GTP, and two for NADH (one catalytic... 

Fig. 2. Reaction of 3 -p-fluorosulfonylbenzoyladenosine with bovine liver glutamate dehydrogenase. Glutamate dehydrogenase (021 mg/ml) was incubated with 3 -FSBA (0.496 mil/) at 24° in 0.01 M sodium barbital buffer (pH 8) containing 0.43 M KCl and 5% ethanol. At each indicated time, an aliquot was withdrawn, diluted 20-fold with Tris-0.1 M acetate buffer (pH 8) at 0°, and assayed (A) in the absence and (B) in the presence of 100 yM ADP. Inset Determination of the pseudo first-order rate constant from the decrease in activation by ADP. (Ft and Fo are the enzymic velocities measured in the presence of ADP and the given and zero time, respectively, and F > is the constant velocity at the end of the reaction. The pseudo first-order rate constant calculated is 0D351 min. ) Data are taken from P. K. Pal, W. J. Wechter, and R. F. Colman, Biochemistry 14, 707 (1975).

Moon, K., and E. L. Smith Sequence of Bovine Liver Glutamate Dehydrogenase. III. Peptides Produced by Specific Chemical Cleavages the Complete Sequence of the Protein. J. Biol. Chem. 238, 3082-3088 (1973). 

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