Nishikata M, Yoshimura F
Central Research Division, School of Dentistry, Hokkaido University, Sapporo, Japan.
Biochem Biophys Res Commun. 1991 Jul 15;178(1):336-42. doi: 10.1016/0006-291x(91)91819-x.
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.
