Inhibition by Lactoferrin and κ-Casein Glycomacropeptide of Binding of Cholera Toxin to its Receptor

TLDR: The competitive binding assay demonstrated that both Lf and GMP inhibited the binding of CT to GM1, although their affinity for CT was lower than that of GM1.

Abstract: Inhibition from binding of Cholera toxin (CT) to Chinese hamster ovary (CHO)-K1 cells and ganglioside GM1 by lactoferrin (Lf) and K-casein glycomacropeptide (GMP) from cow’s milk was examined. Both Lf and GMP effectively reduced the CT-derived morphological changes in CHO-K1 cells. The competitive binding assay demonstrated that both Lf and GMP inhibited the binding of CT to GMH although their affinity for CT was lower than that of GM1. The inhibitory effect of Lf and GMP seemed to be attributed to their terminal sialic acid, although the sugar chain sequence only partially fitted to the CT-receptor.