N-TERMINAL DOMAIN OF PEPSIN AS A MODEL FOR RETROVIRAL DIMERIC ASPARTYL PROTEASE

被引：7

作者：

BIANCHI, M ^{[1
]}

BOIGEGRAIN, RA ^{[1
]}

CASTRO, B ^{[1
]}

COLETTIPREVIERO, MA ^{[1
]}

机构：

[1] INSERM,U58,60 RUE NAVACELLES,F-34100 MONTPELLIER,FRANCE

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 167卷 / 01期

关键词：

D O I：

10.1016/0006-291X(90)91770-S

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：

Autolysis of porcine pepsin at pH 4 affords a derivative possessing intrinsic proteolytic activity. This derivative was isolated by alumina pseudo-affinity chromatography and gel-filtration and was found to result from the tight association of two identical molecules, 135 amino acids long, emerging from the N-terminal domain of pepsin. This finding emphasizes a similarity with the only aspartyl-proteases known to act as dimers, the retroviral proteases. © 1990.

引用

页码：339 / 344

页数：6

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