MECHANISM OF PROTEIN PRECIPITATION AND STABILIZATION BY CO-SOLVENTS

被引：121

作者：

TIMASHEFF, SN

ARAKAWA, T

机构：

[1] Brandeis Univ, United States

来源：

JOURNAL OF CRYSTAL GROWTH | 1988年 / 90卷 / 1-3期

基金：

美国国家卫生研究院;

关键词：

Organic Compounds - Crystallization - Solvents - Thermodynamics;

D O I：

10.1016/0022-0248(88)90296-5

中图分类号：

O7 [晶体学];

学科分类号：

0702 ; 070205 ; 0703 ; 080501 ;

摘要：

The interactions between proteins and a number of substances which, when present at high concentration, stabilize or precipitate proteins, have been analyzed in terms of the preferential interactions of these co-solvents with proteins. In all cases, stabilization or precipitation was accompanied by preferential exclusion of the co-solvent from the immediate domain of the protein, i.e., preferential hydration of the protein. This means that addition of the co-solvent to the aqueous protein solution increased the chemical potentials of both components. The thermodynamic interaction parameters derived from such data make it possible to calculate the salting out constant, ks, as well as to construct a phase isotherm for any given solvent mixture which indicates the limiting protein solubility.

引用

页码：39 / 46

页数：8