title: Characterization of two forms of hemagglutinin/protease produced by Vibrio cholerae non-O1.
abstract: Two forms (34 kDa and 32 kDa) of hemagglutinin/protease produced by Vibrio cholerae non-O1 were characterized. The hemagglutinin/protease purified by immunoaffinity column chromatography using a monoclonal antibody was essentially a 34-kDa form. By incubation of the purified 34-kDa form at 37 degrees C, it was processed (autodigested) to the 32-kDa form. The N-terminal 20 amino acid sequences of both the 34- and 32-kDa forms were identical, suggesting that proteolytic processing at the C-terminal region of the 34-kDa hemagglutinin/protease resulted in the 32-kDa form. With this shift, protease activity increased, but hemagglutinating activity decreased, suggesting that the C-terminal region of the hemagglutinin/protease is related to hemagglutinating activity.
authors.affiliation: Research Institute for Microbial Diseases, Osaka University, Japan.
authors.forename: A
authors.initials: A
authors.lastname: Naka
authors.forename: K
authors.initials: K
authors.lastname: Yamamoto
authors.forename: T
authors.initials: T
authors.lastname: Miwatani
authors.forename: T
authors.initials: T
authors.lastname: Honda
mesh_terms: D000595:Amino Acid Sequence; D010450:Endopeptidases / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D006388:Hemagglutinins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D017386:Sequence Homology, Amino Acid; D014734:Vibrio cholerae / Q000201:enzymology* / Q000235:genetics / Q000276:immunology*
chemical_list: D006388:Hemagglutinins; D010450:Endopeptidases