Characterization of two forms of hemagglutinin/protease produced by Vibrio cholerae non-O1.
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.
Naka
A
A
Research Institute for Microbial Diseases, Osaka University, Japan.
Yamamoto
K
K
Miwatani
T
T
Honda
T
T
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*
D006388:Hemagglutinins; D010450:Endopeptidases