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 language | English |
|---|---|
| Pages (from-to) | 4159-4162 |
| Number of pages | 4 |
| Journal | Infection and Immunity |
| Volume | 58 |
| Issue number | 12 |
| Publication status | Published - 1990 |
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- Immunology
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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 journal › Article
}
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.
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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 -