The Protective Effects of Osmolytes on Yeast Alcohol Dehydrogenase Conformational Stability and Aggregation

被引：2
|
作者：
Han, Hong-Yan [1 ]
Yao, Zhi-Gang [2 ]
Gong, Cheng-Liang [1 ]
Xu, Wei-An [1 ]
机构：
[1] Soochow Univ, Coll Med, Dept Biol, Suzhou 215123, Peoples R China
[2] Binzhou Univ, Dept Life Sci, Binzhou 256603, Shandong, Peoples R China
来源：
PROTEIN AND PEPTIDE LETTERS | 2010年 / 17卷 / 08期
关键词：
Aggregation; conformational stability; osmolytes; transition free energy; unfolding; yeast alcohol dehydrogenase; GLYCINE BETAINE; IN-VITRO; PROTEIN; INACTIVATION; TREHALOSE; ENZYME; UREA; ADDITIVES; ARGININE; KINASE;
D O I：
10.2174/092986610791498902
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 protective effects of four osmolytes (trehalose, dimethysulfoxide, glycine and proline) on the conformational stability and aggregation of guanidine-denatured yeast alcohol dehydrogenase (YADH) have been investigated in this paper. The results show that the four osmolytes protect YADH against unfolding and inactivation by reducing ki (inactivation rate constants), increasing Delta Delta Gi (transition free energy changes at 25 degrees C), increasing Cm (value for the midpoint of denaturation) and decreasing its ANS-binding fluorescence intensity. Furthermore, these osmolytes can prevent YADH aggregation in a concentration-dependent manner during YADH refolding.
引用
收藏
页码：1058 / 1066
页数：9
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