Inhibition by Lactoferrin and<i>κ</i>-Casein Glycomacropeptide of Binding of<i>Cholera</i>Toxin to its Receptor
Yoshihiro Kawasaki, Hiroko Isoda, Morimasa Tanimoto, Shun’ichi Dosako, Tadashi Idota, Kenkichi Ahiko
Bioscience Biotechnology and Biochemistry
Abstract
Inhibition from binding of Cholera toxin (CT) to Chinese hamster ovary (CHO)-K1 cells and ganglioside GM1 by lactoferrin (Lf) and kappa-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 GM1, 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.
Extracted Claims
2 claims extracted from this paper into the knowledge graph
lactoferrin inhibited Cholera toxin binding to GM1
“Both Lf and GMP inhibited the binding of CT to GM1, although their affinity for CT was lower than that of GM1.”
kappa-casein glycomacropeptide inhibited Cholera toxin binding to GM1
“Both Lf and GMP inhibited the binding of CT to GM1, although their affinity for CT was lower than that of GM1.”