REVEALING ACTIVE-SITE ON THE LIGHT SUBUNIT OF PENICILLIN ACYLASE

被引：0

作者：

KABAKOV, VE

KLYACHKO, NL

LEVASHOV, AV

机构：

来源：

BIOCHEMISTRY AND MOLECULAR BIOLOGY INTERNATIONAL | 1995年 / 35卷 / 02期

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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：

Serine-specific irreversible inhibitor phenylmethanesulfonyl fluoride (PMSF) inactivates penicillin acylase subunits, which were chromatographically separated under denaturing conditions and refolded by dialysis, in aqueous solution and Aerosol OT reversed micelles. The activities of both alpha and beta subunits decrease with increasing PMSF concentration but the dependence is no longer linear, in contrast with the native enzyme. The enzyme inactivated in aqueous solution, when solubilized in the micellar system at Wo=12, exhibits an additional activity, which can be further inhibited by PMSF.

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页码：441 / 446

页数：6

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