Chen X C, Hua Z C, Zhu D X
Department of Biochemistry, Nanjing University, China.
Biochem Mol Biol Int. 1996 Jul;39(4):797-803. doi: 10.1080/15216549600201891.
A Gly-Pro-Arg-Pro tetrapeptide, homologous to amino-terminal segment of the human fibrin alpha chain after the release of the fibrinopeptide A, was covalently coupled to peptide A of low molecular weight urokinase. The resulting derivative gained increased affinity for fibrin. In caseinolytic assay, fibrin can stimulate the derivative to activate plasminogen. The derivative had two-fold greater fibrinolytic potency than native low molecular weight urokinase and its affinity for fibrin clot was 3.9-fold higher than that of low molecular weight urokinase.
一种甘氨酰-脯氨酰-精氨酰-脯氨酸四肽,与释放纤维蛋白肽A后人纤维蛋白α链的氨基末端片段同源,与低分子量尿激酶的肽A共价偶联。所得衍生物对纤维蛋白的亲和力增加。在酪蛋白溶解试验中,纤维蛋白可刺激该衍生物激活纤溶酶原。该衍生物的纤溶活性比天然低分子量尿激酶高两倍,其对纤维蛋白凝块的亲和力比低分子量尿激酶高3.9倍。