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火鸡肝脏黄嘌呤脱氢酶:依赖于功能性活性位点含量的酶的特性。

Turkey liver xanthine dehydrogenase: properties of the enzyme dependent on the content of functional active sites.

作者信息

Cleere W F, O'Regan C, Coughlan M P

出版信息

Biochem J. 1974 Nov;143(2):465-8. doi: 10.1042/bj1430465.

Abstract

Turkey liver xanthine dehydrogenase containing the full complement of molybdenum, flavin and iron-sulphur prosthetic groups is, as normally isolated, a mixture of functional and non-functional enzyme. The latter apparently lacks the cyanolysable persulphide groups essential to the oxidation of xanthine and to interaction with arsenite. These groups are not required for the oxidation of NADH by Methylene Blue. That KI treatment effects a differential release of flavin from xanthine-prereduced and NADH-prereduced enzyme merely reflects the degree of functionality of the preparations used and may not be taken as evidence for non-equivalence of the flavin chromophores.

摘要

正常分离得到的含有完整钼、黄素和铁硫辅基的火鸡肝脏黄嘌呤脱氢酶是一种功能性和非功能性酶的混合物。后者显然缺乏黄嘌呤氧化和与亚砷酸盐相互作用所必需的可被氰化物裂解的过硫化物基团。这些基团对于亚甲蓝氧化NADH并非必需。碘化钾处理导致黄素从黄嘌呤预还原和NADH预还原的酶中差异释放,这仅仅反映了所用制剂的功能程度,不能作为黄素发色团不等同的证据。

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Turkey liver xanthine dehydrogenase: further observations on the reaction with arsenite.
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