scholarly journals Characterization of a heat modifiable protein, Escherichia coli outer membrane protein OmpA in binary surfactant system of sodium dodecyl sulfate and octylglucoside

1998 ◽  
Vol 1375 (1-2) ◽  
pp. 101-109 ◽  
Author(s):  
Satoshi Ohnishi ◽  
Keiichi Kameyama ◽  
Toshio Takagi
1998 ◽  
Vol 5 (5) ◽  
pp. 370-382 ◽  
Author(s):  
Sung-Liang Yu ◽  
Hwia-Cheng Ding ◽  
June-Nam Seah ◽  
Kang-Mai Wu ◽  
Yu-Chung Chang ◽  
...  

1998 ◽  
Vol 66 (10) ◽  
pp. 4726-4728 ◽  
Author(s):  
Noboru Nakasone ◽  
Masaaki Iwanaga

ABSTRACT The outer membrane protein OmpU of Vibrio cholerae O1 strain 86B3 was characterized with reference to colonization of the intestine by the organism. The purified OmpU exhibited a pI of 3.6. Upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, it migrated to 38, 32, and 110 kDa when the sample was heated at 100°C for 2 min, 50°C for 15 min, and room temperature for 30 min, respectively. The purified OmpU was not hemagglutinative. Anti-OmpU serum did not agglutinate strain 86B3 or other V. cholerae organisms. OmpU adhered to the brush border of the rabbit small intestine; adhesion of the organisms to the intestine treated in advance with OmpU was not inhibited. Treating the organisms in advance with anti-OmpU Fab did not inhibit adhesion to the intestine. These results obtained in vitro suggest that OmpU is not involved in the adhesion of V. cholerae to the intestinal epithelium.


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