Studies on xanthine oxidase: II. Mechanism of substrate inhibition and its reversal by histamine
Studies on xanthine oxidase: II. Mechanism of substrate inhibition and its reversal by histamine
复制标题
黄嘌呤氧化酶的研究：II．
DOI：
10.1016/0926-6569(63)90105-6
复制
发表时间：
1963
期刊：
影响因子：
--
通讯作者：
S. Muraoka
中科院分区：
文献类型：
--
作者：
S. Muraoka
次黄嘌呤诱导的黄嘌呤氧化酶抑制（见前摘要）被消除的金属离子的去除，并重新出现时，微量的铜，铅，锌，钙和镁加入。当酶，铜，底物和组胺按此顺序加入时，酶是无活性的，但当组胺之前的底物添加抑制没有发生。组胺与次黄嘌呤的拮抗作用为非竞争性。组胺对核黄素荧光或次黄嘌呤对荧光的淬灭没有影响，而Cu++对核黄素荧光有明显的淬灭作用。M.P.H.
The hypoxanthine-induced xanthine oxidase inhibition (see preceding abstract) was eliminated by the removal of metallic ions and reappeared when minute quantities of Cu, Pb, Zn, Ca and Mg were added. When enzyme, Cu, substrate and histamine were added in this order, the enzyme was inactive but when histamine preceded substrate addition inhibition did not occur. The antagonism between histamine and hypoxanthine was non-competitive. Histamine had no effect on riboflavin fluorescence or on the quenching of the fluorescence by hypoxanthine, while Cu++showed marked quenching of riboflavin fluorescence. M.P.H.