The non-immunoglobulin component of human milk responsible for the inhibition of cell adhesion (haemagglutination) mediated by colonisation factor antigen 1 (CFA1) was determined by chromatographic fractionation of human whey proteins with Sephadex G-200, DEAE cellulose and heparin-sepharose. Pure free secretory component (fSC) and pure lactoferrin (Lf) were isolated and both compounds inhibited the haemagglutination induced by CFA1. The lowest concentrations of purified fSC and Lf able to inhibit the haemagglutination induced by strain TR50/3 CFA1 were 0.06 mg/ml and 0.1 mg/ml respectively. Commercially available lactoferrin from human milk and transferrin from human serum, which has a great structural analogy to lactoferrin, also inhibited the haemagglutination. The lowest concentrations of the commercial lactoferrin and transferrin able to inhibit the haemagglutination induced by TR50/3 CFA1 were 0.03 mg/ml and 0.4mg/ml, respectively. These results indicate that fSC and Lf may be important non-specific defence factors against enterotoxigenic infections.


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