Abstract
Detection of heat shock proteins in Vibrio parahaemolyticus was investigated by SDS-PAGE and Western immunoblotting procedure using an anti-Hsp 60 antibody. Results indicate that V. parahaemolyticus elicited at least one Hsp 60 (GroEL)-like protein with apparent molecular weight of about 58,000 (58 kDa) when submitted to a heat shift from 30 to 42 degrees C. Kanagawa phenomenon-positive and -negative strains of V. parahaemolyticus responded the same way. Six other Vibrio species also showed an increased synthesis of GroEL-like (58 kDa) protein after heat shock, while synthesis of 58 kDa protein of V. alginolyticus was at a similar level before and after heat shock. Vibrio nereis showed an increased synthesis of a 60 kDa GroEL-like protein.
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