The effect of the conformation of collagen on its ability to aggregate platelets

Abstract The interaction between platelets and collagen, which marks the initiation of hemostasis, was examined as a function of the conformation and the multimerization of soluble guinea pig skin collagen. Both the rate and extent of collagen multimerization, as measured by the intensity of scattered light, are dependent on the time of incubation and on the temperature of the system. Compounds such as arginine or penicillamine, which at low concentrations ( −2 M) inhibit collagen crosslinking, in higher quantities (> 2 × 10 −2 M) decrease the ability of collagen to form multimers and hence to initiate platelet aggregation. By these techniques we have been able to correlate the initiation of platelet aggregation by collagen with the extent of preformed multimers, the lag time approaching zero as the multimerization of the initiating collagen increases.