Conformational changes and inactivation of calf intestinal alkaline phosphatase in trifluoroethanol solutions

被引：13

作者：

Zhang, YX

Zhu, Y

Zhou, HM ^{[1
]}

机构：

[1] Tsinghua Univ, Dept Biol Sci & Biotechnol, Beijing 100084, Peoples R China

[2] Capital Univ Med Sci, Dept Chem, Beijing 100054, Peoples R China

来源：

INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY | 2000年 / 32卷 / 08期

关键词：

alkaline phosphatase; trifluoroethanol; unfolding; inactivation;

D O I：

10.1016/S1357-2725(00)00025-X

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 changes in activity and unfolding of calf intestinal alkaline phosphatase (CLP) during denaturation in different concentrations of trifluoroethanol (TFE) have been investigated by far-ultraviolet circular dichroism and fluorescence emission spectra. Unfolding and activation rate constants were measured and compared, the activation and inactivation courses were much faster than that of unfolding, which suggests that the active site of CIP containing two zinc ions and one magnesium ion is situated in a limited and flexible region of the enzyme molecule that is more fragile to the denaturant than the protein as a whole. However, compared to other metalloenzymes, CIP is inactivated at higher concentrations of TFE as denaturant. (C) 2000 Elsevier Science Ltd. All rights reserved.

引用

页码：887 / 894

页数：8

共 21 条

[1] Evidence for the existence of an unfolding intermediate state for aminoacylase during denaturation in guanidine solutions [J].