PRESSURE-INDUCED MOLTEN GLOBULE STATE OF CHOLINESTERASE

被引：53

作者：

CLERY, C ^{[1
]}

RENAULT, F ^{[1
]}

MASSON, P ^{[1
]}

机构：

[1] CTR RECH SERV SANTE ARMEES, UNITE BIOCHEM, F-38702 LA TRONCHE, FRANCE

来源：

FEBS LETTERS | 1995年 / 370卷 / 03期

关键词：

CHOLINESTERASE; MOLTEN GLOBULE; PRESSURE; ELECTROPHORESIS;

D O I：

10.1016/0014-5793(95)00787-A

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 denaturing effect of pressure on the structure of human butyrylcholinesterase was examined by gel electrophoresis under pressure and by 8-anilino-1-naphthalene sulfonate (ANS) binding. It was found that the fluorescence intensity of bound ANS is increased by pressure between 0.5 and 1.5 kbar and that the hydrodynamic volume of the enzyme swells when pressures around 1.5 kbar are applied. These findings indicate that pressure denaturation of butyrylcholinesterase is a multi-step process and that the observed transient pressure-denatured states have characteristics of molten globules.

引用

页码：212 / 214

页数：3

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