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[膜双分子层中转运三磷酸腺苷酶的寡聚体组装]

[Oligomeric assemblies of transport adenosine triphosphatases in a membrane bilayer].

作者信息

Boldyrev A A

出版信息

Zh Evol Biokhim Fiziol. 1995 Jul-Aug;31(4):375-86.

PMID:8779277
Abstract

The comparative analysis of the own and literature data concerning the oligomeric organization of membrane-bound transport ATPases is presented. The results show that functional activity of protomeres is distinct from that of oligomeric assembly. It was demonstrated that ATP regulated interprotomer interaction in the oligomers including their dissociation into individual protomers. Evidence for changeable amount of protomers interacting with each other at different stages of the hydrolytic cycle is presented. The hypothesis that membrane lipids regulate the activity of membrane-bound oligomeric proteins affecting the efficiency of interprotomer interactions within the oligomeric complexes is justified.

摘要

本文对膜结合转运ATP酶的寡聚体组织的自身数据和文献数据进行了比较分析。结果表明,亚基的功能活性与寡聚体装配的功能活性不同。已证明ATP调节寡聚体中亚基间的相互作用,包括使其解离成单个亚基。文中提供了在水解循环不同阶段相互作用的亚基数量可变的证据。膜脂通过影响寡聚体复合物中亚基间相互作用的效率来调节膜结合寡聚蛋白活性这一假说得到了验证。

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