Identification and Initial Characterization of Elastase Activity Associated with Vibrio cholerae |
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Authors: | J Michael Janda Sharon L Abbott Shideh Khashe |
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Institution: | (1) Microbial Diseases Laboratory, Division of Communicable Disease Control, California Department of Health Services, 2151 Berkeley Way, Berkeley, CA 94704-1011, USA , US |
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Abstract: | Strains of Vibrio cholerae O1 (Ogawa, Inaba) and non-O1 serogroups have been found to produce an elastolytic protease that can be detected on 0.3% elastin
agar plates or in broth cultures. The elastase enzyme appears to be maximally expressed in late log phase (14–18 h postinoculation)
and has optimum activity at a pH range between 7 and 8. Comparative studies indicate that more than 60% of V. cholerae strains analyzed quantitatively produce more elastase in broth (two- to fourfold higher) than other elastase-positive Vibrio species such as Vibrio vulnificus. The V. cholerae elastase enzyme was not inhibited by trypsin, serine-protease, or thiol-protease inhibitors, but was inhibited by phosphoramidon.
Ultrafiltration studies indicate the V. cholerae elastase enzyme has a molecular weight >30,000, and a 34K protein with possible elastase activity has been detected by SDS-PAGE
for one non-O1 isolate (strain 2396). Cumulative results suggest that the V. cholerae elastase is probably a member of the N-type metalloprotease family and shares similar properties with other elastase enzymes
described for pathogenic and nonpathogenic species in this genus.
Received: 26 February 1999 / Accepted: 29 March 1999 |
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