Increased catalytic activity of protein disulfide isomerase using aromatic thiol based redox buffers

被引：11

作者：

Gough, JD

Lees, WJ ^{[1
]}

机构：

[1] Florida Int Univ, Dept Chem & Biochem, Miami, FL 33199 USA

[2] Syracuse Univ, Dept Chem, Syracuse, NY 13244 USA

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2005年 / 15卷 / 03期

基金：

美国国家科学基金会;

关键词：

protein folding; PDI; RNase A; aromatic thiols; thiol-disulfide interchange reaction;

D O I：

10.1016/j.bmcl.2004.11.005

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

PDI is an enzyme that acts as a chaperone, shufflase, and oxidase during the folding of disulfide-containing proteins. The ability of aromatic thiols to increase the activity of PDI-catalyzed protein folding over that of the standard thiol glutathione (GSH) was measured. 4-Mercaptobenzoic acid (ArSH) increased the activity of PDI by a factor of three. (C) 2004 Elsevier Ltd. All rights reserved.

引用

收藏

页码：777 / 781

页数：5

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