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Radiation-induced changes in purified prothrombin and thrombin

L P Chanderkar, G B Nadkarni

    Biochimica Et Biophysica Acta
    |August 23, 1982
    PubMed
    Summary

    Gamma irradiation damages purified prothrombin and thrombin proteins. Clotting activity is more sensitive to radiation than esterase function, with prothrombin being more affected than thrombin.

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    Area of Science:

    • Biochemistry
    • Radiation Biology
    • Protein Chemistry

    Background:

    • Prothrombin and thrombin are critical coagulation factors.
    • Understanding radiation effects on proteins is vital for various applications.

    Purpose of the Study:

    • To investigate the impact of gamma irradiation on purified prothrombin and thrombin.
    • To assess radiation-induced changes in their clotting and esterase activities, structure, and kinetics.

    Main Methods:

    • Purified prothrombin and thrombin were subjected to gamma irradiation.
    • Clotting and esterase activities were measured.
    • Physicochemical properties including spectral characteristics, amino acid composition, and electrophoretic mobility were analyzed.

    Main Results:

    • Clotting activity was more susceptible to gamma radiation than esterase function for both proteins.
    • Prothrombin was more sensitive to radiation than thrombin.
    • Irradiation of prothrombin reduced thrombin formation, while thrombin's clotting activity was significantly impaired, affecting tyrosine, tryptophan, and histidine residues.

    Conclusions:

    • Gamma irradiation differentially affects prothrombin and thrombin, with clotting function being more vulnerable.
    • Structural modifications, particularly of specific amino acid residues, underlie the observed functional changes.
    • These findings have implications for radiation processing and understanding protein stability.

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