主要结构的单链pro-urokinase。

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开赛,Arimura H, Nishida M, Suyama T

主要结构的单链pro-urokinase。

生物化学杂志。1985年10月5日;260 (22):12382 - 9。

PubMed ID

2931434 (在PubMed

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文摘

单链pro-urokinase是一个人类与一个单链尿激酶活性的酶原形式的结构和50000先生和催化转化为主动two-chain形式,大量的胞浆素。这是隔绝人类肾脏细胞的培养液和受到化学(CNBr)和蛋白水解(lysyl肽链内切酶)退化。由此产生的肽被反相高效液相色谱分离,进行自动序列分析。氨基酸序列的85% 411年17肽残留恢复被发现是一致的(157个氨基酸)和B链链(253个氨基酸)的人类尿激酶Gunzler报道和同事(Gunzler, w。·斯蒂芬斯,G.J.ot, F。、金、S.-M。,一个。Frankus E。,Flohe l . (1982) Hoppe-Seyler z .杂志。化学。363年,133 - 141;1155 - 1165;·斯蒂芬斯,G.J.Gunzler,西澳ot, F。, Frankus, E., and Flohe, L. (1982) Hoppe-Seyler's Z. Physiol. Chem. 363, 1043-1058). It revealed the presence of Lys at position 158 in single-chain pro-urokinase through which the two polypeptide chains of human urokinase are unified into one molecule. In addition, firm evidence was found that upon activation by plasmin single-chain pro-urokinase is cleaved at the Lys-Ile bond between residues 158 and 159, resulting in the formation of a two-chain urokinase molecule held together by one disulfide linkage. These results indicate that the cleavage at the Lys-Ile bond between residues 158 and 159 is responsible for conformational change, appearance of enzyme activity and reduction of its high affinity for fibrin.

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尿激酶