CHARACTERIZATION OF PORPHYROMONAS (BACTEROIDES) GINGIVALIS HEMAGGLUTININ AS A PROTEASE

被引：71

作者：

NISHIKATA, M ^{[1
]}

YOSHIMURA, F ^{[1
]}

机构：

[1] AICHI GAKUIN UNIV,SCH DENT,DEPT MICROBIOL,NAGOYA 464,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 178卷 / 01期

关键词：

D O I：

10.1016/0006-291X(91)91819-X

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：

A hemagglutinin (HA) was purified to homogeneity from the membrane fraction of the oral bacterium Porphyromonas gingivalis. The HA possessed protease activity hydrolyzing proteins and arginine-containing synthetic substrates. The protease activity was inhibited by thiol-blocking reagents, and hence the HA can be characterized as a cystein protease. The HA functions as an attachment factor and its substrate-binding site is responsible for the attachment to an erythrocyte. © 1991.

引用

页码：336 / 342

页数：7

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