Edwards Y H, Potter J, Hopkinson D A
Biochem J. 1980 May 1;187(2):429-36. doi: 10.1042/bj1870429.
A newly discovered human diaphorase, designated diaphorase-4, which accounts for a major part of the diaphorase activity of most tissues but does not occur in erythrocytes, is described. In contrast with other human diaphorases, it is dependent on FAD for activity after electrophoresis, inhibited by low concentrations of dicoumarol and shows a marked affinity for Cibacron Blue. The molecular weight was estimated to be 49000 +/- 1800 by gel filtration. Diaphorase-4 appears to show person-to-person quantitative variation, so that about 4% of the population lack appreciable enzyme activity, but it is not yet clear whether this variation is of genetic or non-genetic origin.
本文描述了一种新发现的人类黄递酶，命名为黄递酶-4。它在大多数组织的黄递酶活性中占主要部分，但在红细胞中不存在。与其他人类黄递酶不同，电泳后其活性依赖于黄素腺嘌呤二核苷酸（FAD），低浓度双香豆素可抑制其活性，并且对汽巴克隆蓝有显著亲和力。通过凝胶过滤法估计其分子量为49000±1800。黄递酶-4似乎存在个体间的定量差异，约4%的人群缺乏明显的酶活性，但这种差异是遗传起源还是非遗传起源尚不清楚。
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