A large number of similarities have previously been noted between the blood and milk clotting phenomena [Jollès, P. (1975) Mol. Cell. Biochem. 7, 73-85; Jollès, P. & Henschen, A. (1982) Trends Biochem. Sci. 7, 325-328]: some analogous features have also been found between fibrinogen and kappa-casein. In this connection, the effect of a natural and a synthetic peptide derived from kappa-casein on platelet function was studied: the undecapeptide Met-Ala-Ile-Pro-Pro-Lys-Lys-Asn-Gln-Asp-Lys (residues 106----116 of cow kappa-casein) inhibited both aggregation of ADP-treated platelets and binding of 125I-fibrinogen to ADP-treated platelets: its behaviour was similar to that of the structurally related C-terminal dodecapeptide of human fibrinogen gamma-chain.
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