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  • Title: Kinetics of hydrolysis of peptide thioester derivatives of arginine by human and bovine thrombins.
    Author: Cook RR, McRae BJ, Powers JC.
    Journal: Arch Biochem Biophys; 1984 Oct; 234(1):82-8. PubMed ID: 6486828.
    Abstract:
    Several peptide thioester substrates have been synthesized and tested with human thrombins (alpha, gamma, and nitrated), bovine thrombin, trypsin, and Factor X alpha beta. The substrates include various thioalkyl esters, thiobenzyl esters with substitution in the 4-position, substrates containing additional residues on the amino-terminal side of the scissile bond (P extended substrates) and one substrate containing additional residues on the carboxyl-terminal side (P' extended substrate). Neither the P nor the P' extensions resulted in significantly increased specificity; however, with one P extended substrate, D-Phe-Pro-Arg-SBzl, the KM with bovine thrombin (0.72 microM) was the second lowest KM yet reported. The results of this study underscore the importance of P vs. P' extension for thrombin substrates. The kinetic constants of the thiobenzyl esters were found to be little affected by the 4-position substitutions. A comparison of gamma-thrombin and nitrothrombin shows them to be quite similar kinetically, while both are significantly less reactive than alpha-thrombin. With these substrates, trypsin, bovine thrombin, and Factor X alpha beta have kcat/KM values in the approximate ratio of 35:10:1, respectively. The results presented here should be of value in the future design of reactive yet specific substrates for thrombin. The comparisons between the various enzymes could be helpful in clarifying the nature of their active sites.
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