| Autor: |
Faming, Dong, Shimodori, Shoichi, Moriya, Tetsuhiro, Iwanaga, Sadaaki, Amako, Kazunobu |
| Zdroj: |
Microbiology and Immunology; November 1993, Vol. 37 Issue: 11 p861-868, 8p |
| Abstrakt: |
A substance cryoprotective for Vibrio choleraeon the prawn shell surface was purified by ammonium sulfate precipitation and gel filtration. It was a protein of 81 kDa and called cryoprotective protein (CPP). The cryoprotective activity of this protein for V. choleraewas sensitive to heat at 100 C and trypsin treatment. In the presence of Mg ion the protein can bind to the bacterial cell surface. V. choleraecan adhere to the shell surface of the prawn. The number of adhered bacteria was reduced by treating the shell with anti‐CPP serum, heat or by trypsin. The presence of Mg ion promoted the adherence. These results suggest that the CPP could serve as an adherence site for V. choleraeon the shell surface. |
| Databáze: |
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