Influence of osmolytes on inactivation and aggregation of muscle glycogen phosphorylase b by guanidine hydrochloride.: Stimulation of protein aggregation under crowding conditions

被引：24

作者：

Eronina, TB ^{[1
]}

Chebotareva, NA ^{[1
]}

Kurganov, BI ^{[1
]}

机构：

[1] Russian Acad Sci, Bach Inst Biochem, Moscow 119071, Russia

来源：

BIOCHEMISTRY-MOSCOW | 2005年 / 70卷 / 09期

基金：

俄罗斯基础研究基金会;

关键词：

muscle glycogen phosphorylase b; guanidine hydrochloride; inactivation; aggregation; osmolyte;

D O I：

10.1007/s10541-005-0219-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The effects of the osmolytes trimethylamine-N-oxide (TMAO), betaine, proline, and glycine on the kinetics of inactivation and aggregation of rabbit skeletal muscle glycogen phosphorylase b by guanidine hydrochloride (GuHCl) have been studied. It is shown that the osmolytes TMAO and betaine exhibit the highest protective efficacy against phosphorylase b inactivation. A test system for studying the effects of macromolecular crowding induced by osmolytes on aggregation of proteins is proposed. TMAO and glycine increase the rate of phosphorylase b aggregation induced by GuHCl.

引用

页码：1020 / 1026

页数：7

共 52 条

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