RELATIONSHIP BETWEEN SURFACE HYDROPHILICITY OF A PROTEIN AND ITS STABILITY AGAINST DENATURATION BY ORGANIC-SOLVENTS

被引：66

作者：

KHMELNITSKY, YL ^{[1
]}

BELOVA, AB ^{[1
]}

LEVASHOV, AV ^{[1
]}

MOZHAEV, VV ^{[1
]}

机构：

[1] MV LOMONOSOV STATE UNIV,DEPT CHEM,MOSCOW 119899,USSR

来源：

FEBS LETTERS | 1991年 / 284卷 / 02期

关键词：

CHYMOTRYPSIN; ORGANIC SOLVENT; ENZYME DENATURATION; ENZYME MODIFICATION;

D O I：

10.1016/0014-5793(91)80700-D

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 stability of alpha-chymotrypsin covalently modified with a strongly hydrophilic modifier, pyromellitic dianhydride, against solvent-induced denaturation in water-organic solvent binary mixtures has been studied. It was found that the hydrophilization results in a strong stabilization of the enzyme against denaturation by organic solvents. The stabilizing effect is explained in terms of the enhanced ability of the hydrophilized enzyme to keep its hydration shell, which is indispensable for supporting the native protein conformation, from denaturing stripping by organic solvents.

引用

页码：267 / 269

页数：3

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