Detection of Hsp60 (Gro-EL)-like proteins in Vibrio parahaemolyticus and Vibrio species by western immunoblotting analysis.
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.
Koga
T
T
Department of Food Microbiology, Tokushima University School of Medicine, Japan.
Nakajyo
Y
Y
Komoto
A
A
D015153:Blotting, Western; D018834:Chaperonin 60 / Q000032:analysis*; D008970:Molecular Weight; D014733:Vibrio / Q000737:chemistry*; D014736:Vibrio parahaemolyticus / Q000737:chemistry*
D018834:Chaperonin 60