Gershkovich A A, Podlipskiĭ V Ia, Kostiuchenko N V, Karabut L I, Kibirev V K
Ukr Biokhim Zh (1978). 1995 Jan-Feb;67(1):57-64.
In order to study the interactions of synthetic substrates with the active site of thrombin the compounds of R-CO-Abz-Arg-OMe were obtained which contained, o-, m- and p-amino benzoic acids (Abz) at P2-subsite. R-CO-moiety was butyric, perfluorobutyric, benzoyl, 2-fluorobenzoyl and perfluorobenzoyl groups. Kinetic parameters of their hydrolysis by thrombin were measured and antithrombin activity was studied. Introduction of fluorine atoms into N-acyl groups caused insignificant alterations of the substrate or inhibitor properties of the compounds containing N-butyric group, but significantly influenced the substrate properties, when peptides contained N-benzoyl group. The interaction mechanism of the obtained substrates with thrombin was proposed.
为了研究合成底物与凝血酶活性位点的相互作用，制备了R-CO-Abz-Arg-OMe化合物，其在P2亚位点含有邻、间和对氨基苯甲酸（Abz）。R-CO部分为丁酸、全氟丁酸、苯甲酰基、2-氟苯甲酰基和全氟苯甲酰基。测定了它们被凝血酶水解的动力学参数，并研究了抗凝血酶活性。将氟原子引入N-酰基中，对于含有N-丁酰基的化合物，其底物或抑制剂性质变化不显著，但当肽含有N-苯甲酰基时，会显著影响底物性质。提出了所得底物与凝血酶的相互作用机制。
