Alikulov Z A, L'vov N P, Burikhanov S S, Kretovich V L
Biol Bull Acad Sci USSR. 1980 Sep-Oct;7(5):379-84.
A quantitative method for the anaerobic isolation of a molybdenum cofactor from two molybdenum-containing enzymes, nitrate reductase from the bacteroids of lupine nodules and xanthine oxidase from milk, is described. It was established that the cofactor consists of an aromatic component and a number of amino acid residues bound to it. The structural and catalytic function of the molybdenum cofactor in the enzyme was established.
本文描述了一种从两种含钼酶（羽扇豆根瘤类菌体中的硝酸还原酶和牛奶中的黄嘌呤氧化酶）中厌氧分离钼辅因子的定量方法。已确定该辅因子由一个芳香族成分和与之结合的若干氨基酸残基组成。还确定了钼辅因子在酶中的结构和催化功能。
