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Antithrombin activity of the hirudin N‐terminal core domain residues 1–43
Author(s) -
Chang Jui-Yoa,
Schlaeppi Jean-Marc,
Stone Stuart R.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80105-r
Subject(s) - hirudin , antithrombin , chemistry , terminal (telecommunication) , thrombin , biochemistry , domain (mathematical analysis) , stereochemistry , heparin , medicine , computer science , platelet , computer network , mathematics , mathematical analysis
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 (Lys 47 ), 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.