Kagitani H, Tagawa M, Hatanaka K, Ikari T, Saito A, Bando H, Okada K, Matsuo O
FEBS Lett. 1985 Sep 9;189(1):145-9. doi: 10.1016/0014-5793(85)80860-7.
Tissue-type plasminogen activator (t-PA) has a high affinity for fibrin and induces lysis of fibrin (fibrinolysis) on the surface of fibrin without degrading circulating fibrinogen. cDNA for t-PA which lacks the 'finger-domain' (the site for fibrin affinity) was isolated from Detroit 562 cells. Analysis of the nucleotide sequence revealed a lack of the sequences which code for the finger-domain. A plasmid (pDPAT 1) containing the Escherichia coli tac promoter/operator and the cDNA sequence coding for 'finger-domain lacking t-PA' was constructed for expression in E. Coli. The polypeptide so produced was a new type of t-PA lacking finger-domain, but revealed plasminogen activator activity with the function of fibrin affinity.
组织型纤溶酶原激活剂（t-PA）对纤维蛋白具有高亲和力，并能在纤维蛋白表面诱导纤维蛋白溶解（纤溶作用），而不会降解循环中的纤维蛋白原。从底特律562细胞中分离出了缺乏“指状结构域”（纤维蛋白亲和力位点）的t-PA的cDNA。对核苷酸序列的分析显示，编码指状结构域的序列缺失。构建了一个含有大肠杆菌tac启动子/操纵子以及编码“缺乏指状结构域的t-PA”的cDNA序列的质粒（pDPAT 1），用于在大肠杆菌中表达。如此产生的多肽是一种新型的缺乏指状结构域的t-PA，但具有纤维蛋白亲和力功能的纤溶酶原激活剂活性。
