Open AccessCharacterization of two forms of hemagglutinin/protease produced by Vibrio cholerae non‐O1
Author(s) -
Naka Atsuko,
Yamamoto Koichiro,
Miwatani Toshio,
Honda Takeshi
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05513.x
Subject(s) - vibrio cholerae , hemagglutinin (influenza) , microbiology and biotechnology , protease , vibrionaceae , chemistry , biology , virology , bacteria , virus , biochemistry , enzyme , genetics
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.