Thermodynamics and kinetics for hirudin binding to human α-, β- and γ-thrombin, under experimental conditions which mimic the in vivo conditions (i.e., pH = 7.35, T = 37.0°C, I = 0.1 M), indicate that the inhibitor specificity for the three species of the enzyme is different. Such a finding agrees with the human thrombin:hirudin binding geometry as revealed by X-ray crystal studies. From the therapeutic viewpoint, thermodynamics and kinetics here reported indicate that the inhibitory activity of hirudin in vivo is more effective than that shown by antithrombin III, which is generally considered the most important plasma thrombin inhibitor.
|Translated title of the contribution||Inhibition of human thrombin activity by hirudin|
|Number of pages||2|
|Journal||Medicina - Rivista della Enciclopedia Medica Italiana|
|Publication status||Published - 1990|
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