Identification and initial characterization of elastase activity associated with Vibrio cholerae.

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.

journal_name

Curr Microbiol

journal_title

Current microbiology

authors

Janda JM,Abbott SL,Khashe S

doi

10.1007/s002849900421

keywords:

subject

Has Abstract

pub_date

1999-08-01 00:00:00

pages

73-8

issue

2

eissn

0343-8651

issn

1432-0991

pii

CM3010

journal_volume

39

pub_type

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