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Chondroitin sulphates (CSs) were isolated from the intima and the media of normal (normal CSs) and atherosclerotic (sclerotic CSs) regions of human aortas. Normal and sclerotic CSs accelerated the inactivation of thrombin by antithrombin III to an equal extent. By this mechanism, both normal and sclerotic CSs prolonged thrombus formation time in a moving stream of platelet-rich plasma and thrombin-catalysed clotting time of platelet-poor plasma. However, anticoagulant activity of sclerotic CSs in thrombin-catalysed fibrin clot formation in platelet-poor plasma was lower than that of normal CSs. The lower anticoagulant activity of sclerotic CSs was due to the greater accelerating effect on the polymerization of monomeric fibrin to form clot, which was the final distinguishable step of fibrinogen-fibrin conversion.
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