Purification and characterization of a protease produced by Vibrio mimicus

M. A R Chowdhury, Shin-ichi Miyoshi, S. Shinoda

Research output: Contribution to journalArticle

44 Citations (Scopus)

Abstract

A protease produced by Vibrio mimicus was purified to apparent homogeneity by ammonium sulfate fractionation and successive column chromatography on Sephacryl S-100 and Mono Q Monobeads. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (PAGE) of the final preparation of the enzyme revealed the homogeneity of the purified enzyme. Conventional PAGE showed that the purified protease migrated as a single band with protease activity. The molecular weight of the protease was estimated to be about 31,000 on the basis of its mobility on sodium dodecyl sulfate-PAGE. The purified protease had both proteolytic and hemagglutination (HA) activities. The proteolytic and HA activities were inhibited by metalloprotease inhibitors and heat treatment. V. mimicus protease therefore appeared as a heat-labile, bifunctional molecule capable of mediating proteolysis and HA. The immunodiffusion analysis showed that the proteases produced by Vibrio cholerae and V. mimicus are immunologically cross-reactive.

Original languageEnglish
Pages (from-to)4159-4162
Number of pages4
JournalInfection and Immunity
Volume58
Issue number12
Publication statusPublished - 1990

Fingerprint

Vibrio mimicus
Peptide Hydrolases
Hemagglutination
Polyacrylamide Gel Electrophoresis
Sodium Dodecyl Sulfate
Hot Temperature
Vibrio cholerae
Immunodiffusion
Ammonium Sulfate
Metalloproteases
Enzymes
Proteolysis
Chromatography
Molecular Weight

ASJC Scopus subject areas

  • Immunology

Cite this

Purification and characterization of a protease produced by Vibrio mimicus. / Chowdhury, M. A R; Miyoshi, Shin-ichi; Shinoda, S.

In: Infection and Immunity, Vol. 58, No. 12, 1990, p. 4159-4162.

Research output: Contribution to journalArticle

Chowdhury, M. A R ; Miyoshi, Shin-ichi ; Shinoda, S. / Purification and characterization of a protease produced by Vibrio mimicus. In: Infection and Immunity. 1990 ; Vol. 58, No. 12. pp. 4159-4162.
@article{b3ab3ed8b51e4c4489195181b9d74049,
title = "Purification and characterization of a protease produced by Vibrio mimicus",
abstract = "A protease produced by Vibrio mimicus was purified to apparent homogeneity by ammonium sulfate fractionation and successive column chromatography on Sephacryl S-100 and Mono Q Monobeads. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (PAGE) of the final preparation of the enzyme revealed the homogeneity of the purified enzyme. Conventional PAGE showed that the purified protease migrated as a single band with protease activity. The molecular weight of the protease was estimated to be about 31,000 on the basis of its mobility on sodium dodecyl sulfate-PAGE. The purified protease had both proteolytic and hemagglutination (HA) activities. The proteolytic and HA activities were inhibited by metalloprotease inhibitors and heat treatment. V. mimicus protease therefore appeared as a heat-labile, bifunctional molecule capable of mediating proteolysis and HA. The immunodiffusion analysis showed that the proteases produced by Vibrio cholerae and V. mimicus are immunologically cross-reactive.",
author = "Chowdhury, {M. A R} and Shin-ichi Miyoshi and S. Shinoda",
year = "1990",
language = "English",
volume = "58",
pages = "4159--4162",
journal = "Infection and Immunity",
issn = "0019-9567",
publisher = "American Society for Microbiology",
number = "12",

}

TY - JOUR

T1 - Purification and characterization of a protease produced by Vibrio mimicus

AU - Chowdhury, M. A R

AU - Miyoshi, Shin-ichi

AU - Shinoda, S.

PY - 1990

Y1 - 1990

N2 - A protease produced by Vibrio mimicus was purified to apparent homogeneity by ammonium sulfate fractionation and successive column chromatography on Sephacryl S-100 and Mono Q Monobeads. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (PAGE) of the final preparation of the enzyme revealed the homogeneity of the purified enzyme. Conventional PAGE showed that the purified protease migrated as a single band with protease activity. The molecular weight of the protease was estimated to be about 31,000 on the basis of its mobility on sodium dodecyl sulfate-PAGE. The purified protease had both proteolytic and hemagglutination (HA) activities. The proteolytic and HA activities were inhibited by metalloprotease inhibitors and heat treatment. V. mimicus protease therefore appeared as a heat-labile, bifunctional molecule capable of mediating proteolysis and HA. The immunodiffusion analysis showed that the proteases produced by Vibrio cholerae and V. mimicus are immunologically cross-reactive.

AB - A protease produced by Vibrio mimicus was purified to apparent homogeneity by ammonium sulfate fractionation and successive column chromatography on Sephacryl S-100 and Mono Q Monobeads. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (PAGE) of the final preparation of the enzyme revealed the homogeneity of the purified enzyme. Conventional PAGE showed that the purified protease migrated as a single band with protease activity. The molecular weight of the protease was estimated to be about 31,000 on the basis of its mobility on sodium dodecyl sulfate-PAGE. The purified protease had both proteolytic and hemagglutination (HA) activities. The proteolytic and HA activities were inhibited by metalloprotease inhibitors and heat treatment. V. mimicus protease therefore appeared as a heat-labile, bifunctional molecule capable of mediating proteolysis and HA. The immunodiffusion analysis showed that the proteases produced by Vibrio cholerae and V. mimicus are immunologically cross-reactive.

UR - http://www.scopus.com/inward/record.url?scp=0025681660&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025681660&partnerID=8YFLogxK

M3 - Article

C2 - 2254038

AN - SCOPUS:0025681660

VL - 58

SP - 4159

EP - 4162

JO - Infection and Immunity

JF - Infection and Immunity

SN - 0019-9567

IS - 12

ER -