螯合剂对人肝脏醛脱氢酶的作用。
The action of chelating agents on human liver aldehyde dehydrogenase.
作者信息
Sidhu R S, Blair A H
出版信息
Biochem J. 1975 Nov;151(2):443-5. doi: 10.1042/bj1510443.
Abstract
Human liver aldehyde dehydrogenase was inhibited by aromatic chelating agents. However, structurally related compounds with much lower metal-complexing ability displayed affinities for enzyme essentially equal to those of their respective chelating analogues. Inhibition was competitive with respect to the coenzyme. It is suggested that hydrophobic interactions between the inhibitors and the coenzyme-binding site of the enzyme are responsible for the observed effects on activity.
摘要
人肝脏醛脱氢酶受到芳香族螯合剂的抑制。然而，具有低得多的金属络合能力的结构相关化合物对该酶的亲和力基本上与其各自的螯合类似物相同。抑制作用相对于辅酶而言是竞争性的。有人提出，抑制剂与酶的辅酶结合位点之间的疏水相互作用是观察到的对活性产生影响的原因。
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本文引用的文献
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Computer programmes for processing enzyme kinetic data.用于处理酶动力学数据的计算机程序。
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Complex formation of 1,10-phenanthroline with zinc ions and the zinc of alcohol dehydrogenase of horse liver.1,10-菲咯啉与锌离子以及马肝醇脱氢酶中的锌形成配合物。
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Differential chemical reactivities of zinc in horse liver alcohol dehydrogenase.马肝醇脱氢酶中锌的不同化学反应活性
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