Characterization of Porphyromonas (bacteroides) gingivalis hemagglutinin as a protease.
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.
Nishikata
M
M
Central Research Division, School of Dentistry, Hokkaido University, Sapporo, Japan.
Yoshimura
F
F
D001439:Bacteroides / Q000201:enzymology* / Q000276:immunology; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D006388:Hemagglutinins / Q000302:isolation & purification*; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000494:pharmacology; D013379:Substrate Specificity; D014107:Tosyllysine Chloromethyl Ketone / Q000494:pharmacology
D006388:Hemagglutinins; D011480:Protease Inhibitors; D014107:Tosyllysine Chloromethyl Ketone; D010450:Endopeptidases