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Interaction of α 2 ‐macroglobulin‐bound thrombin with hirudin
Author(s) -
Pochon François,
Steinbuch Marion
Publication year - 1984
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(84)80991-6
Subject(s) - hirudin , thrombin , dissociation constant , chemistry , covalent bond , discovery and development of direct thrombin inhibitors , dissociation (chemistry) , alpha 2 macroglobulin , binding site , stereochemistry , biochemistry , macroglobulin , platelet , receptor , biology , immunology , organic chemistry
The human thrombin bound to α 2 ‐macroglobulin (α 2 M) in a 1:1 stoichiometry is still able to interact with one of its specific inhibitors, hirudin. The dissociation constant of the complex hirudin‐α 2 M‐bound thrombin is 1 × 10 −7 M, whatever the mode of thrombin binding, covalent or non‐covalent.