Abstract
Vibrio vulnificus, an opportunistic human pathogen, secretes the 50 kDa single-chain hemolysin. When incubated with an exocellular protease from this vibrio, the 50 kDa hemolysin was cleaved in some peptides joined with the disulfide bond(s); the 40 kDa fragment and the small fragment(s) undetectable in SDS-PAGE. The nicked hemolysin induced comparable hemolysis through the same process as that of the intact toxin. However, the nicked hemolysin was found to be more stable against inactivation due to autoaggregation, so that it formed a larger precipitation zone in the single radial immunodiffusion test using the antiserum against the intact hemolysin. These results suggest thatV. vulnificushemolysin is modified to be a more hydrophilic protein by nicking, while it is not accompanied by loss of the hemolytic activity.
Published Version
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