PURIFICATION OF PENICILLIN-INSENSITIVE DD-ENDOPEPTIDASE, A NEW CELL-WALL PEPTIDOGLYCAN-HYDROLYZING ENZYME IN ESCHERICHIA-COLI, AND ITS INHIBITION BY DEOXYRIBONUCLEIC ACIDS

被引：31

作者：

TOMIOKA, S

MATSUHASHI, M

机构：

[1] Institute of Applied Microbiology, University of Tokyo, Bunkyo-ku, Tokyo

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1978年 / 84卷 / 04期

关键词：

D O I：

10.1016/0006-291X(78)91679-0

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：

Activity of a penicillin-insensitive DD-endopeptidase that splits the D-alanyl-meso-2,6-diaminopimelyl linkage in peptidoglycan was demonstrated in a sonic extract of Escherichia coli. The protein with this activity was partially purified. The activity was inhibited by 3 μg per ml of deoxyribonucleic acid, suggesting that this cell wall hydrolytic enzyme is regulated by deoxyribonucleic acid or its fragments. © 1978.

引用

页码：978 / 984

页数：7

共 8 条

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