The functional domain of hirudin, a thrombin‐specific inhibitor

FEBS Letters

Chang, Jui-Yoa¹ 

[1] Pharmaceuticals Research Laboratories, Ciba-Geigy Ltd. Basel CH-4002, Switzerland

关键词: Hirudin;    Tyrosine sulfate;    Micro C-terminal sequencing;    Thrombin specificity;    DABITC;    dimethylaminoazobenzene isothiocyanate;    DABS-Cl;    dimethylaminoazobenzenesulfonyl chloride;   

DOI  :  10.1016/0014-5793(83)80307-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Hirudin is a thrombin-specific of M _r 8000 (65 amino acid residues). Native hirudin contains 3 disulfide linkages within the first 39 amino-terminal residues, and highly C-terminal segment which is freely accessible to enzyme digestion by both endo- and exo-peptidases. Removal of the acidic C-terminal amino acids of native hirudin by both chemical and enzymatic methods resulted in a concomitant loss of hirudin inhibition activity. It is concluded that this acidic C-terminal segment of hirudin is essential for hirudin—thrombin interaction. The implication of the hirudin—thrombin interaction for the enzymatic specificity of thrombin is also discussed.

【 授权许可】

Unknown