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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 49 (1988), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The hemagglutinating activity of the heat-labile enterotoxin (LTp) isolated from porcine enterotoxigenic Escherichia coli was studied by hemagglutination inhibition. The hemagglutinating activity of LTp was enhanced 64–512-fold with pronase- and neuraminidase-treated human erythrocytes although both intact human and sheep erythrocytes were not agglutinated by LTp at the highest concentration used. No enhancement was found in hemagglutination of neuraminidase-treated sheep erythrocytes by LTp. Hemagglutination of pronase-treated human type A erythrocytes induced by LTp was inhibited by melibiose and galactose among mono-, di-, and polysaccharides used as inhibitors. Galactose was a slightly better inhibitor than melibiose. These findings suggest that LTp is a bacterial lectin specific for galactose.
    Type of Medium: Electronic Resource
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