ANTITHROMBIN ACTIVITY OF THE HIRUDIN N-TERMINAL CORE DOMAIN RESIDUES 1-43

被引:23
作者
CHANG, JY
SCHLAEPPI, JM
STONE, SR
机构
[1] Pharmaceuticals Research Laboratories, Ciba-Geigy Ltd.
[2] Friedrich Mieschler Institute
关键词
Hirudin; Hirudin fragment; Hirudin-thrombin interaction;
D O I
10.1016/0014-5793(90)80105-R
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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 Ki 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. © 1990.
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页码:209 / 212
页数:4
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