| Abstract: | The capacity of methyl esters of arginine-containing substrates to inhibit the proteolytic activity of thrombin is studied. A relationship between the structure of peptides and their capacity to inhibit the thrombin-fibrinogen reaction is investigated. Parameters Ks, k2 and k3, which characterize individual stages of the protein process are calculated from experimentally obtained kcat, Km and I50 values. It is shown that the antithrombin activity of peptides becomes maximal only in the case when residues of hydrophobic amino acids would be simultaneously present both at the positions of P2 and P3 of oligopeptides. |
