期刊论文详细信息
FEBS Letters | |
Antithrombin activity of the hirudin N‐terminal core domain residues 1–43 | |
Stone, Stuart R.1  Chang, Jui-Yoa2  Schlaeppi, Jean-Marc2  | |
[1] Friedrich Mieschler Institute, CH-4002 Basel, Switzerland;Pharmaceuticals Research Laboratories, Ciba-Geigy Ltd., CH-4002 Basel, Switzerland | |
关键词: Hirudin; Hirudin fragment; Hirudin-thrombin interaction; | |
DOI : 10.1016/0014-5793(90)80105-R | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Hirudin N-terminal core domain residues 1–43 (r-Hir1–43) were prepared from limited proteolysis of recombinant hirudin by V8 Staphylococcal protease followed by purification with reversed-phase HPLC. r-Hir1-43 lacks the putative reactive site of hirudin (Lys47), but binds to thrombin (with K i of 300 nM) and blocks the catalytic activity of the protease. The structural element which accounts for the thrombin inhibitory activity of r-Hir1–43 is analyzed in this report.
【 授权许可】
Unknown
【 预 览 】
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