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Serine protease specificity for peptide chromogenic substrates.

L E Mattler, N U Bang

    Thrombosis and Haemostasis
    |December 15, 1977
    PubMed
    Summary

    New synthetic peptide substrates show promise for studying blood clotting enzymes and inhibitors. These chromogenic substrates offer specificity for enzymes like thrombin, factor Xa, and plasmin, aiding clinical diagnostics.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Clinical Diagnostics

    Background:

    • Development of novel synthetic peptide chromogenic substrates for enzyme activity assessment.
    • Need for specific and sensitive tools to study plasma serine proteases and their inhibitors.

    Purpose of the Study:

    • Evaluate the substrate specificity of newly developed chromogenic peptides (S-2160, S-2238, S-2222, S-2251, Chromozym TH, Chromozym PK).
    • Determine the sensitivity of these substrates to purified human and bovine enzymes: plasmin, trypsin, thrombin, and factor Xa.
    • Develop diagnostic assays for key hemostatic and fibrinolytic factors and inhibitors.

    Main Methods:

    • Hydrolysis rate assays using purified enzymes (plasmin, trypsin, thrombin, factor Xa) and chromogenic peptide substrates.
    • Evaluation of substrate specificity and sensitivity.
    • Development of enzyme-linked assays for antithrombin III, heparin, plasminogen/plasmin inhibitors, and prekallikrein/kallikrein inhibitors.

    Main Results:

    • S-2160, S-2238, and Chromozym TH are sensitive to thrombin, with Chromozym TH and S-2238 showing higher sensitivity.
    • S-2222 is specific for factor Xa, while S-2251 demonstrates plasmin specificity, including enhanced sensitivity to the SK-plasmin complex.
    • Chromozym PK is relatively specific for plasma kallikrein, enabling the development of various diagnostic assays.

    Conclusions:

    • The evaluated synthetic peptide substrates are sensitive and relatively specific tools for studying plasma serine proteases.
    • These substrates are applicable to kinetic and clinical studies of enzymes like thrombin, factor Xa, plasmin, and kallikrein.
    • The developed assays facilitate the study of critical components of the hemostasis and fibrinolysis systems.

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