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Related Experiment Videos

The isolation of human platelet factor V.

R W Viskup, P B Tracy, K G Mann

    Blood
    |April 1, 1987
    PubMed
    Summary

    Human platelet factor V is stored in platelets as a fragmented procofactor. Thrombin cleavage activates this platelet factor V into its active form, platelet factor Va, essential for the prothrombinase complex.

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    Area of Science:

    • Biochemistry
    • Hematology
    • Molecular Biology

    Background:

    • Human platelet factor V (PFV) is a crucial component of the prothrombinase complex.
    • Its relationship to plasma factor V and its native form within platelets require further elucidation.

    Purpose of the Study:

    • To characterize the structure and activation of human platelet factor V.
    • To determine if platelet factor V is stored as a procofactor and how it is activated.

    Main Methods:

    • Isolation of human platelet factor V using monoclonal and polyclonal antibodies.
    • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for molecular weight analysis.
    • Immunoblotting and bioassays to assess protein structure and function.

    Main Results:

    • Purified platelet factor V consists of peptides with apparent molecular weights ranging from 115 K to 330 K, indicating fragmentation.
    • These fragments are immunologically related to plasma factor V.
    • Platelet factor V is a procofactor that, upon thrombin cleavage, yields active platelet factor Va, indistinguishable from plasma factor Va.

    Conclusions:

    • Human platelet factor V is stored within platelets in a partially fragmented procofactor state.
    • Activation by thrombin converts platelet factor V to the active platelet factor Va, a key player in hemostasis.

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