Yamagishi R, Koide T, Sakuragawa N
Central Clinical Laboratory, Toyama Medical and Pharmaceutical University, Japan.
FEBS Lett. 1987 Dec 10;225(1-2):109-12. doi: 10.1016/0014-5793(87)81140-7.
Heparin cofactor II (HC II) and thrombin were chemically modified with pyridoxal 5'-phosphate, and their effects on the inhibition of thrombin by HC II in the presence of heparin or dermatan sulfate were studied. The inhibition of thrombin by HC II was enhanced about 7000-fold in the presence of heparin or dermatan sulfate. However, this enhancement by heparin dwindled to 110- and 9.6-fold when the modified HC II and the modified thrombin, respectively, were substituted for native proteins. Essentially identical results were obtained from the experiments using dermatan sulfate. These results indicate that the binding of heparin or dermatan sulfate to both thrombin and HC II is required for the sulfated polysaccharide-dependent acceleration of the thrombin inhibition by HC II, and the binding to thrombin is more essential for the reaction.
用5'-磷酸吡哆醛对肝素辅因子II(HC II)和凝血酶进行化学修饰,并研究了在肝素或硫酸皮肤素存在下它们对HC II抑制凝血酶的影响。在肝素或硫酸皮肤素存在下,HC II对凝血酶的抑制作用增强了约7000倍。然而,当分别用修饰的HC II和修饰的凝血酶替代天然蛋白质时,肝素的这种增强作用分别降至110倍和9.6倍。使用硫酸皮肤素进行的实验获得了基本相同的结果。这些结果表明,HC II对凝血酶的硫酸化多糖依赖性加速抑制作用需要肝素或硫酸皮肤素与凝血酶和HC II两者结合,并且与凝血酶的结合对该反应更为重要。