Abstract
Some properties and mechanism of action of a hemolysin (VMH) produced by an enteropathogenic Vibrio mimicus strain was examined. VMH was heat-labile and inhibited by addition of divalent cations, including Ca2+, Mg2+ and Mn2+. The hemolysis by VMH was inhibited by incubating with gangliosides, suggesting that the ganglioside was the binding site on the erythrocyte membrane for VMH. Existence of a galactose moiety on reducing end of the ganglioside molecule and a sialic acid on the galactose moiety was suggested to be important for the binding of VMH molecule. Colloid osmotic manner of the hemolysis by VMH was demonstrated.
| Original language | English |
|---|---|
| Pages (from-to) | 405-409 |
| Number of pages | 5 |
| Journal | Microbiology and Immunology |
| Volume | 37 |
| Issue number | 5 |
| Publication status | Published - 1993 |
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Keywords
- gangliosides
- hemolysin
- Vibrio mimicus
ASJC Scopus subject areas
- Immunology and Microbiology(all)
- Microbiology
- Microbiology (medical)
Cite this
Studies on hemolytic action of a hemolysin produced by Vibrio mimicus. / Shinoda, S.; Ishida, K.; Oh, E. G.; Sasahara, K.; Miyoshi, Shin-ichi; Chowdhury, M. A R; Yasuda, T.
In: Microbiology and Immunology, Vol. 37, No. 5, 1993, p. 405-409.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Studies on hemolytic action of a hemolysin produced by Vibrio mimicus
AU - Shinoda, S.
AU - Ishida, K.
AU - Oh, E. G.
AU - Sasahara, K.
AU - Miyoshi, Shin-ichi
AU - Chowdhury, M. A R
AU - Yasuda, T.
PY - 1993
Y1 - 1993
N2 - Some properties and mechanism of action of a hemolysin (VMH) produced by an enteropathogenic Vibrio mimicus strain was examined. VMH was heat-labile and inhibited by addition of divalent cations, including Ca2+, Mg2+ and Mn2+. The hemolysis by VMH was inhibited by incubating with gangliosides, suggesting that the ganglioside was the binding site on the erythrocyte membrane for VMH. Existence of a galactose moiety on reducing end of the ganglioside molecule and a sialic acid on the galactose moiety was suggested to be important for the binding of VMH molecule. Colloid osmotic manner of the hemolysis by VMH was demonstrated.
AB - Some properties and mechanism of action of a hemolysin (VMH) produced by an enteropathogenic Vibrio mimicus strain was examined. VMH was heat-labile and inhibited by addition of divalent cations, including Ca2+, Mg2+ and Mn2+. The hemolysis by VMH was inhibited by incubating with gangliosides, suggesting that the ganglioside was the binding site on the erythrocyte membrane for VMH. Existence of a galactose moiety on reducing end of the ganglioside molecule and a sialic acid on the galactose moiety was suggested to be important for the binding of VMH molecule. Colloid osmotic manner of the hemolysis by VMH was demonstrated.
KW - gangliosides
KW - hemolysin
KW - Vibrio mimicus
UR - http://www.scopus.com/inward/record.url?scp=0027197720&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027197720&partnerID=8YFLogxK
M3 - Article
C2 - 8355623
AN - SCOPUS:0027197720
VL - 37
SP - 405
EP - 409
JO - Microbiology and Immunology
JF - Microbiology and Immunology
SN - 0385-5600
IS - 5
ER -