Inhibition of Escherichia coli heat-labile enterotoxin by an amino carbonyl product, lactose-alpha-lactalbumin.

The inhibition by lactose-alpha-lactalbumin amino carbonyl product of Escherichia coli heat-labile enterotoxin was studied by GM1-ELISA and by assay with CHO-K1 cells. The product dose-dependently inhibited the binding of the enterotoxin to GM1 ganglioside and decreased the morphological change of CHO-K1 cells caused by this toxin. The results suggest that this product may be a receptor analogue in the intestine.