血小板纤维蛋白原。其纤溶酶降解模式的鉴定及初步观察。

Platelet fibrinogen. Identity and initial observations on the mode of its degradation by plasmin.

作者信息

James H L, Bradford H R, Ganguly P

出版信息

Biochim Biophys Acta. 1975 Mar 28;386(1):209-20. doi: 10.1016/0005-2795(75)90261-5.

Abstract

Fibrinogen has been purified from human platelets. Platelet fibrinogen exhibits a characteristic pattern in agar gel immunoelectrophoresis different from that of plasma fibrinogen. Stepwise plasmin degradation has been used in further elucidation of the molecular properties of the platelet protein. Examination of comparative digests by immunologic and gel electrophoretic methods has revealed that (1) the platelet protein is more resistant to plasmin degradation, (2) the plasmin-produced fragments of platelet fibrinogen differ consistently from those of its plasma counterpart, and (3) platelet fibrinogen is different from fragment X of plasma fibrinogen. It is suggested that platelet fibrinogen may contribute to the stability of the thrombus.

摘要

纤维蛋白原已从人血小板中纯化出来。血小板纤维蛋白原在琼脂凝胶免疫电泳中呈现出与血浆纤维蛋白原不同的特征模式。逐步进行的纤溶酶降解已被用于进一步阐明血小板蛋白的分子特性。通过免疫和凝胶电泳方法对比较性消化产物的检查表明：（1）血小板蛋白对纤溶酶降解更具抗性；（2）血小板纤维蛋白原经纤溶酶产生的片段与其血浆对应物的片段始终不同；（3）血小板纤维蛋白原与血浆纤维蛋白原的X片段不同。有人提出，血小板纤维蛋白原可能有助于血栓的稳定性。