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一项关于肝脏分支酶催化反应的研究。

A study of the reaction catalysed by the liver branching enzyme.

作者信息

Verhue W, Hers H G

出版信息

Biochem J. 1966 Apr;99(1):222-7. doi: 10.1042/bj0990222.

Abstract

The mechanism of action of liver branching enzyme has been studied by using as substrate two polysaccharides in which the non-reducing ends had been labelled by incubation with phosphorylase and a trace amount of [(14)C]glucose 1-phosphate. After these polysaccharides had been treated with branching enzyme, their structure was analysed by periodate oxidation, by degradation with phosphorylase and amylo-(1-->6)-glucosidase and by degradation with pullulanase. All the results indicate that the branching enzyme catalyses the transfer from (1-->4)- to (1-->6)-linkage of a chain of glucose units, the minimum length of which is six glucose units. A maltodextrin containing 16 glucose units was not acted on by the branching enzyme.

摘要

通过使用两种多糖作为底物来研究肝脏分支酶的作用机制,这两种多糖的非还原端已通过与磷酸化酶和微量[(14)C]葡萄糖1-磷酸一起温育进行了标记。在用分支酶处理这些多糖后,通过高碘酸氧化、用磷酸化酶和淀粉-(1→6)-葡萄糖苷酶降解以及用支链淀粉酶降解来分析它们的结构。所有结果表明,分支酶催化葡萄糖单位链从(1→4)-连接向(1→6)-连接的转移,其最短长度为六个葡萄糖单位。含有16个葡萄糖单位的麦芽糊精不会被分支酶作用。

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