Smith A, Nuiry I, Morgan W T
Thromb Res. 1985 Dec 1;40(5):653-61. doi: 10.1016/0049-3848(85)90303-2.
Plasmin and kallikrein but not thrombin cleave purified histidine-rich glycoprotein (HRG), and heparin binding inhibits the proteolysis of HRG. To assess the proteolysis of HRG in plasma, immunoaffinity chromatography was used to isolate HRG from human plasma samples and the extent of protein cleavage was determined after electrophoresis under reduced, denaturing conditions. In blood drawn into streptokinase or into urokinase, HRG (78 kDa) was degraded producing peptides ranging in apparent molecular weight from 67 to 9 kDa. In patients undergoing thrombolytic therapy almost no intact HRG remains after 30 minutes, but the levels of circulating HRG are unchanged, indicating that cleaved HRG is not quickly or extensively removed from the circulation.
纤溶酶和激肽释放酶而非凝血酶可裂解纯化的富含组氨酸糖蛋白（HRG），并且肝素结合可抑制HRG的蛋白水解。为了评估血浆中HRG的蛋白水解情况，采用免疫亲和色谱法从人血浆样本中分离HRG，并在还原、变性条件下进行电泳后测定蛋白质裂解程度。在注入链激酶或尿激酶的血液中，HRG（78 kDa）被降解，产生表观分子量从67 kDa到9 kDa不等的肽段。在接受溶栓治疗的患者中，30分钟后几乎没有完整的HRG残留，但循环中HRG的水平未变，这表明裂解后的HRG不会迅速或大量地从循环中清除。
