Abstract
Derivatives of benzamidine inhibit competitively the activity of the serine proteinases trypsin, plasmin, thrombin, and of the clotting factor Xa. The inhibitor activities (Ki-values) of various benzamidine derivatives against the several enzymes were compared. Besides parallels, deviations in the corresponding structure-activity relationships were found. From these results it is concluded that the similar enzymes exhibit certain differences in the structure of the primary and secondary binding sites.
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