Karabashian L V, Agadzhanian S A, Danoian K V, Kazarian R A
Bioorg Khim. 1988 Nov;14(11):1495-501.
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.
牛肝谷氨酸脱氢酶（L-谷氨酸-NAD(P)-氧化还原酶，EC 1.4.1.3）及其放射性磷酸吡哆醛衍生物通过不同程度的溴化氰活化共价固定在琼脂糖CL-4B上。研究了固定化酶样品的催化和调节特性。结果表明，当用少量溴化氰（每1 ml凝胶少于5 mg）活化琼脂糖时，酶通过六聚体的单个亚基固定。在这种情况下，固定化不会改变谷氨酸脱氢酶的催化和调节特性。固定化的谷氨酸脱氢酶放射性磷酸吡哆醛衍生物完全模仿了固定化的天然酶，可作为谷氨酸脱氢酶催化活性六聚体结构和功能研究的便捷模型。
