title: Possibility of Bacteroides gingivalis hemagglutinin possessing protease activity revealed by inhibition studies.
abstract: Inhibition of hemagglutinin (HA) activity in a membrane fraction of Bacteroides gingivalis was examined using various compounds. Leupeptin and anti-pain inhibited the HA activity at nM order. This potency was lost when the aldehyde group of leupeptin was converted to an alcohol moiety. Irreversible protease inhibitors, tosyl-L-lysine chloromethyl ketone (TLCK), p-chloromercuribenzoate (PCMB), and N-ethylmaleimide (NEM) were also inhibitory. From the inhibition experiments, we speculate that the HA possesses protease activity and that the same site of the molecule participates in the erythrocyte binding and the substrate binding.
authors.affiliation: Central Research Division, School of Dentistry, Hokkaido University.
authors.forename: M
authors.initials: M
authors.lastname: Nishikata
authors.forename: F
authors.initials: F
authors.lastname: Yoshimura
authors.forename: Y
authors.initials: Y
authors.lastname: Nodasaka
mesh_terms: D001439:Bacteroides / Q000201:enzymology* / Q000648:ultrastructure; D001586:Benzoylarginine Nitroanilide / Q000378:metabolism; D006385:Hemagglutination Inhibition Tests; D006388:Hemagglutinins / Q000378:metabolism*; D007976:Leupeptins / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology
chemical_list: D006388:Hemagglutinins; D007976:Leupeptins; D011480:Protease Inhibitors; D001586:Benzoylarginine Nitroanilide; D010447:Peptide Hydrolases; C032854:leupeptin