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Isolation and partial characterization of human factor V.

P A Bolhuis, T B Hakvoort, K Breederveld

    Biochimica Et Biophysica Acta
    |May 23, 1979
    PubMed
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    Researchers purified human Factor V (FV) from plasma using mild techniques. The isolated FV showed high specific activity and was activated by thrombin, indicating its biological relevance.

    Area of Science:

    • Biochemistry
    • Hematology
    • Protein Chemistry

    Background:

    • Factor V (FV) is a crucial protein in the blood coagulation cascade.
    • Understanding FV's structure and function is vital for hemostasis research.
    • Previous purification methods may have altered FV's native properties.

    Purpose of the Study:

    • To isolate and characterize human Factor V (FV) using a novel, mild purification protocol.
    • To determine the molecular properties of purified FV.
    • To assess the functional activation of purified FV.

    Main Methods:

    • Factor V isolation from human citrate plasma via cryoprecipitation and polyethylene glycol fractionation.
    • Gel filtration (AcA 44) and haptoglobin adsorption for purification.

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  • Size exclusion chromatography and ultracentrifugation for molecular weight and sedimentation analysis.
  • Polyacrylamide gel electrophoresis (PAGE) and sodium dodecyl sulfate-PAGE (SDS-PAGE) for purity assessment.
  • Thrombin activation assays.

    • Main Results:

    • Factor V was purified to a specific activity of 14.5 unit/mg with a 28% yield.
    • Purified FV exhibited a molecular weight of 296,000 Da and a sedimentation constant of 7.8 S.
    • Electrophoresis confirmed a single protein band, indicating high purity.
    • Incubation with thrombin resulted in an 8-fold activation of the purified Factor V.

    Conclusions:

    • A mild and effective method for purifying human Factor V was established.
    • The purified Factor V retains its native molecular characteristics and biological activity.
    • This purified FV is suitable for further functional and structural studies in coagulation research.