Characterization of two forms of hemagglutinin/protease produced by Vibrio cholerae non-O1
- 1 November 1992
- journal article
- research article
- Published by Oxford University Press (OUP) in FEMS Microbiology Letters
- Vol. 98 (1-3) , 197-200
- https://doi.org/10.1016/0378-1097(92)90155-h
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°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 the 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.Keywords
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