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[肌浆网钙泵温度解偶联机制:酶分子功能特性及结构状态的变化]

[Mechanism of temperature uncoupling of the sarcoplasmic reticulum calcium pump: change in the functional properties and structural state of the enzyme molecule].

作者信息

Geĭmonen E R, Rubtsov A M, Boldyrev A A

出版信息

Biokhimiia. 1993 Aug;58(8):1296-306.

PMID:8399778
Abstract

The effect of short-term thermal treatment causing the uncoupling of the hydrolytic and transport functions of skeletal muscle sarcoplasmic reticulum Ca-ATRase on the conformational state of the enzyme and the physico-chemical characteristics of the membrane lipid bilayer has been studied. It has been found that enhanced passive permeability of the membrane for Ca2+ is the main cause for the decreased efficiency of the Ca-pump function. Thermal treatment induced no changes in the conformation of the hydrophilic domain of the Ca-ATRase; however, the accessibility of the transmembrane hydrophobic domain for some solutes turned out to be restricted, the microviscosity of the lipid bilayer decreased and the protein-lipid and protein-protein interactions within the membrane disturbed after the heat exposure.

摘要

研究了短期热处理导致骨骼肌肌浆网Ca-ATP酶的水解和转运功能解偶联对酶的构象状态和膜脂双层物理化学特性的影响。结果发现,膜对Ca2+被动通透性增强是Ca泵功能效率降低的主要原因。热处理未引起Ca-ATP酶亲水结构域构象的变化;然而,热暴露后,跨膜疏水结构域对某些溶质的可及性受到限制,脂双层的微粘度降低,膜内蛋白质-脂质和蛋白质-蛋白质相互作用受到干扰。

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