EQUILIBRIUM UNFOLDING OF CLASS-PI GLUTATHIONE-S-TRANSFERASE

被引：57

作者：

DIRR, HW ^{[1
]}

REINEMER, P ^{[1
]}

机构：

[1] MAX PLANCK INST BIOCHEM,W-8033 MARTINSRIED,GERMANY

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 180卷 / 01期

关键词：

D O I：

10.1016/S0006-291X(05)81291-4

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 equilibrium unfolding transition of class π glutathione S-transferase, a homodimeric protein, from porcine lung was monitored by spectroscopic methods (fluorescence emission and ultraviolet absorption ), and by enzyme activity changes. Solvent(guanidine hydrochloride and urea)-induced denaturation is well described by a two-state model involving significant populations of only the folded dimer and unfolded monomer. Neither a folded, active monomeric form nor stable unfolding intermediates were detected. The conformational stability, ΔGu(H2O), of the native dimer was estimated to be about 25.3 ± 2 kcal/mol at 20°C and pH6.5. © 1991 Academic Press, Inc.

引用

页码：294 / 300

页数：7

共 17 条

[1]

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