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Immunochemical studies on factor V

A C Greenquist, R M Weinberg, A L Kuo

    European Journal of Biochemistry
    |October 1, 1975
    PubMed
    Summary
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    Bovine factor V, a crucial blood clotting protein, exists in various molecular forms. Researchers identified its two main subunits, light and heavy chains, aiding in understanding its complex structure and function.

    Area of Science:

    • Biochemistry
    • Hematology
    • Immunology

    Background:

    • Native bovine factor V has a molecular weight of 300,000.
    • Purification reveals multiple factor V molecular weight forms, from fragments to aggregates.
    • Factor V activity is linked to protein bands after electrophoresis.

    Purpose of the Study:

    • To characterize the molecular properties and subunit composition of bovine factor V.
    • To investigate the antigenicity and cross-reactivity of factor V and its subunits.

    Main Methods:

    • Gel filtration and isoelectric focusing to determine molecular weight and isoelectric point.
    • Polyacrylamide gel electrophoresis and immunoelectrophoresis for protein analysis.
    • Antisera production and characterization for immunological studies.

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    Main Results:

    • Purified factor V shows diverse molecular forms, including aggregates and fragments.
    • Isoelectric focusing identified a single peak at pH 4.65 for high-molecular-weight species.
    • Factor V comprises light (73,000) and heavy (125,000) subunits; antisera recognize both.
    • Cross-reactivity observed in sheep and goat plasma, but not monkey or human.

    Conclusions:

    • Bovine factor V exhibits complex molecular heterogeneity during purification.
    • The protein consists of distinct light and heavy subunits, with specific antigenic properties.
    • Antibodies against factor V subunits demonstrate cross-reactivity in certain animal species.