Antithrombin activity of the hirudin N‐terminal core domain residues 1–43

FEBS Letters

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-Hir^1–43) were prepared from limited proteolysis of recombinant hirudin by V8 Staphylococcal protease followed by purification with reversed-phase HPLC. r-Hir^1-43 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-Hir^1–43 is analyzed in this report.

【 授权许可】

Unknown