| Literature DB >> 2069573 |
Abstract
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.Entities:
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Year: 1991 PMID: 2069573 DOI: 10.1016/0006-291x(91)91819-x
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575