INTERMOLECULAR DEGRADATION OF SIGNAL PEPTIDASE-I INVITRO

被引：21

作者：

TALARICO, TL ^{[1
]}

DEV, IK ^{[1
]}

BASSFORD, PJ ^{[1
]}

RAY, PH ^{[1
]}

机构：

[1] UNIV N CAROLINA,SCH MED,DEPT MICROBIOL & IMMUNOL,CHAPEL HILL,NC 27514

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 181卷 / 02期

关键词：

D O I：

10.1016/0006-291X(91)91240-D

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：

Highly purified preparations of signal peptidase I (36 kDa) were found to undergo an apparent inter-autocatalytic degradation at 4°C and 37° C. The disappearance of the 36 kDa protein coincided with the stable appearance of a 31 kDa and a 5 kDa species. Amino-terminal sequencing of the 31 kDa product indicated a site specific cleavage following Ala38-Gln-Ala of signal peptidase I. The 31 kDa fragment was purified and shown to have 100-fold less activity than the native enzyme, with pre-maltose binding protein as a substrate. © 1991.

引用

页码：650 / 656

页数：7

共 31 条

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