Abstract
The characteristics of the binding of biotinylated E. coli K88ab fimbriae to guinea pig erythrocyte membranes, as a possible model of the target host cell were studied. Binding showed sigmoidal dependence, with an apparent saturation at about 0.8 ng of fimbriae. Hill coefficient values ( h) were about 2–2.4, which indicated that the receptor population showed positive cooperativity with at least three binding sites. Apparent binding constants to the first and third binding sites ( 1K 3 and 3K 3) were determined. Three K88ab binding proteins, of 67, 63 and 48 kDa, were identified on solubilized erythrocyte membranes and were recovered mainly in a detergent phase, suggesting a possible integral localization of the receptors.
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