Cryoinactivation and conformational drift of glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle

被引：3
|
作者：
Tian, SM [1 ]
Ruan, KC [1 ]
机构：
[1] Acad Sinica, Shanghai Inst Biochem, Shanghai 200031, Peoples R China
来源：
BIOLOGICAL CHEMISTRY | 1998年 / 379卷 / 11期
基金：
中国国家自然科学基金;
关键词：
conformational drift; cryoinactivation; glyceraldehyde-3-phosphate dehydrogenase;
D O I：
10.1515/bchm.1998.379.11.1319
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 cryoinactivation of glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle (GAPDH-rabbit) was studied. It was found that the inactivation of GAPDH-rabbit at 0 degrees C was much faster than that of GAPDH from yeasts, and showed obvious time and concentration dependence. The spectral properties, enzyme activity and behavior under pressure, of GAPDH-rabbit treated either by cryoinactivation, or pressure-induced dissociation and reassociation, were very similar. These results provided evidence to support the idea that cryoinactivation of oligomeric proteins, might take place through a cycle of dissociation-reassociation accompanied with the so-called conformational drift postulated by King and Weber (1986).
引用
收藏
页码：1319 / 1322
页数：4
相关论文
共 50 条
12345