Refolding of denatured trichosanthin in the presence of GroEL

被引：5

作者：

Lau, CK ^{[1
]}

Wong, RNS

Lo, SCL

Kwok, F

机构：

[1] Univ Tennessee, Dept Biochem, Knoxville, TN 37996 USA

[2] Baptist Univ, Dept Biol, Kowloon Tong, Hong Kong

[3] Hong Kong Polytech Univ, Dept Appl Biol & Chem Technol, Kowloon, Hong Kong

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1998年 / 245卷 / 01期

关键词：

D O I：

10.1006/bbrc.1998.8191

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 stability of trichosanthin (TCS), a 27-kDa ribosome-inactivating protein, was investigated in the presence of guanidinium chloride (GdnHCl). The process of unfolding was monitored by CD and fluorescence spectroscopy, Both methods show the presence of partially folded intermediates. Unfolding of TCS is attained in BM GdnHCl, but the inactive species recover a good deal of its DNase activity upon dilution with buffer containing GroEL and ATP, The mechanism of recognition of unfolded TCS by GroEL was studied by fluorescence spectroscopy. (C) 1998 Academic Press.

引用

页码：149 / 154

页数：6

共 12 条

[1] FLUORESCENCE PROPERTIES OF O-AMINOBENZOYL-LABELED PROTEINS [J].