Kanaide H, Uranishi T, Nakashima Y, Nakamura M
Br J Exp Pathol. 1982 Feb;63(1):82-7.
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.
从人主动脉正常区域（正常硫酸软骨素）和动脉粥样硬化区域（硬化硫酸软骨素）的内膜和中膜中分离出硫酸软骨素（CSs）。正常硫酸软骨素和硬化硫酸软骨素同等程度地加速抗凝血酶III对凝血酶的灭活。通过这种机制，正常硫酸软骨素和硬化硫酸软骨素均延长了富含血小板血浆流动状态下的血栓形成时间以及贫血小板血浆的凝血酶催化凝血时间。然而，在贫血小板血浆中，硬化硫酸软骨素在凝血酶催化纤维蛋白凝块形成过程中的抗凝活性低于正常硫酸软骨素。硬化硫酸软骨素较低的抗凝活性是由于其对单体纤维蛋白聚合成凝块具有更强的加速作用，这是纤维蛋白原 - 纤维蛋白转化的最后一个可区分步骤。
