B. Chabance et al., BINDING OF THE BOVINE CASEINOGLYCOPEPTIDE TO THE PLATELET MEMBRANE GLYCOPROTEIN GPIB-ALPHA, Biochemistry and molecular biology international, 42(1), 1997, pp. 77-84
The bovine caseinoglycopeptide (residues 106-169), the C-terminal part
of kappa-casein, inhibited the von Willebrand factor-dependent platel
et aggregation in a dose-dependent manner. An affinity matrix made of
the caseinoglycopeptide selectively bound the platelet membrane glycop
rotein GPIb alpha which contains the von Willebrand factor binding sit
e. The amino acid residues of GPIb alpha participating in the caseinog
lycopepride binding were located after residue Glu(90).