[Structural organization of glutamate dehydrogenase hexamer. 1. Immobilization on sepharose as a model for analysis of structural-functional characteristics of the enzyme].
Bovine liver glutamate dehydrogenase (L-glutamate-NAD(P)-oxidoreductase, EC 1.4.1.3) and its radioactive phosphopyridoxyl derivative were covalently immobilized on Sepharose CL-4B with different degrees of cyanogen bromide activation. The catalytical and regulatory properties of the immobilized samples of the enzymes were studied. It was shown that the enzymes were immobilized through a single subunit of hexamer when sepharose was activated by small amounts of cyanogen bromide (less than 5 mg per 1 ml of gel). In this case, the immobilization did not alter the catalytical and regulatory properties of glutamate dehydrogenase. The immobilized radioactive phosphopyridoxyl derivative of glutamate dehydrogenase completely imitated the immobilized native enzyme and can be used as a convenient model for structural and functional investigation of catalytically active hexamer of glutamate dehydrogenase.
Karabashian
L V
LV
Agadzhanian
S A
SA
Danoian
K V
KV
Kazarian
R A
RA
D000818:Animals; D002384:Catalysis; D002417:Cattle; D004800:Enzymes, Immobilized; D005969:Glutamate Dehydrogenase; D008099:Liver / Q000201:enzymology; D008954:Models, Biological; D011487:Protein Conformation; D012685:Sepharose
D004800:Enzymes, Immobilized; D012685:Sepharose; D005969:Glutamate Dehydrogenase
Strukturnaia organizatsiia geksamera glutamatdegidrogenazy. 1. Immobilizatsiia na sefaroze s tsel'iu polucheniia modeli dlia izucheniia strukturno-funktsional'nykh osobennosteĭ fermenta.