Enzyme destruction by a protease contaminant in bacitracin

被引：22

作者：

Rogelj, S ^{[1
]}

Reiter, KJ

Kesner, L

Li, M

Essex, D

机构：

[1] New Mexico Tech, Dept Biol, Socorro, NM 87801 USA

[2] SUNY Hlth Sci Ctr, Dept Biochem, Brooklyn, NY 11203 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2000年 / 273卷 / 03期

关键词：

bacitracin; bacitracin impurity; protease; subtilisin; protease inhibitor; protein disulfide isomerase;

D O I：

10.1006/bbrc.2000.3029

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：

Bacitracin, as purchased from biochemical supply companies, is a mixture of more than 30 different substances. The major antibiotic isoforms A and B account for about 60% of the mixture. A newly identified impurity in some, but not all, of the bacitracin lots is a powerful subtilisin-type protease capable of cleaving many proteins including protein disulfide isomerase (PDI), myosin, and a variety of artificial substrates Thus, it is important for investigators who use bacitracin as a protease or other enzyme inhibitor to determine if the bacitracin they are using is contaminated with a protease enzyme. If it is present, they may have to reinterpret their results and retest with an enzyme-free bacitracin reagent. (C) 2000 Academic Press.

引用

收藏

页码：829 / 832

页数：4

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