Effects of polyethylene glycol on stability of α-chymotrypsin in aqueous ethanol solvent

被引：22

作者：

Simon, LM ^{[1
]}

Kotormán, M

Szabó, A

Garab, G

Laczko, I

机构：

[1] Univ Szeged, Fac Sci, Dept Biochem, H-6720 Szeged, Hungary

[2] Hungarian Acad Sci, Biol Res Ctr, Inst Plant Biol, Szeged, Hungary

[3] Hungarian Acad Sci, Biol Res Ctr, Inst Biophys, H-6701 Szeged, Hungary

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2004年 / 317卷 / 02期

基金：

匈牙利科学研究基金会;

关键词：

alpha-chymotrypsin; stability; secondary and tertiary structures; ethanol;

D O I：

10.1016/j.bbrc.2004.03.087

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 polyethylene glycol (PEG) of different molecular weights (400, 2000, 6000, 12,000, 20,000, and 35,000) on the conformational stability and catalytic activity of alpha-chymotrypsin in 60% ethanol were studied. The inactivation caused by the organic solvent was not influenced by PEG 400. However, the PEGs with higher molecular weights up to 35,000 increased the stability of the enzyme, but this alpha-chymotrypsin stabilizing effect was molecular weight-independent. With increase of the molecular weight of PEG, a more stable tertiary structure of the enzyme was observed. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：610 / 613

页数：4

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