Primary structure of human alpha 2-antiplasmin, a serine protease inhibitor (serpin).
Primary structure of human alpha 2-antiplasmin, a serine protease inhibitor (serpin).
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人 α2-抗纤溶酶(一种丝氨酸蛋白酶抑制剂 (serpin))的一级结构。
DOI:
10.1016/s0021-9258(19)75687-7
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发表时间:
1987
期刊:
影响因子:
--
通讯作者:
D. Collen
中科院分区:
文献类型:
--
作者:
W. Holmes;L. Nelles;H. Lijnen;D. Collen
The plasma protein alpha 2-antiplasmin is the main physiological inhibitor of the serine protease plasmin, which is responsible for the dissolution of fibrin clots. We have determined the primary structure of mature human alpha 2-antiplasmin by DNA sequencing of overlapping cDNA fragments prepared from human liver mRNA. cDNA clones were identified by hybridization with a 48-base pair deoxyoligonucleotide probe deduced from the sequence of a 16-amino acid peptide of alpha 2-antiplasmin. Mature human alpha 2-antiplasmin contains 452 amino acids. It is homologous (23-28%) with five other proteins belonging to the serine protease inhibitor (serpin) superfamily. Its reactive site, i.e. the peptide bond cleaved by reaction with its primary target enzyme, plasmin, consists of Arg364-Met365. This dipeptide corresponds to the reactive site Met358-Ser359 of the archetypal serpin, alpha 1-antitrypsin.