The inhibition mode of ulinastatin was indicated noncompetitive by the Lineweaver-Burk's double reciprocal plotting method using the production rate of fibrinopeptide A. Consequently Km of alpha-thrombin could be calculated 2.8 mM and its Vmax was reduced from 24 U/l to 15 U/l by the addition of ulinastatin and Ki of ulinastatin was 1.05 x 10(-2) M. The complex of ulinastatin and alpha-thrombin were found. Furthermore, the mixing of alpha-thrombin, AT-III and ulinastatin produced a larger complex on SDS-PAGE at pH 7.0, and it was evident by the use of Western blotting method, that the complex was consisted of alpha-thrombin, AT-III and ulinastatin. Although ulinastatin and thrombomodulin showed multiple similarities in inhibitory functions on alpha-thrombin, still there are some differences functioning on alpha-thrombin, because of the different binding sites of ulinastatin and thrombomodulin on alpha-thrombin, indicating no crossreaction for antithrombomodulin monoclonal antibody relating to alpha-thrombin binding site of thrombomodulin and it could be contributed to form noncompetitive or uncompetitive inhibitors.
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