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Bovine factor v: a calcium-containing metalloprotein

A C Greenquist, R W Colman

    Blood
    |November 1, 1975
    PubMed
    Summary
    This summary is machine-generated.

    Factor V binds tightly to phospholipids, even without calcium. Chelators inhibit factor V activity by binding to its calcium, suggesting phospholipids complex at this calcium site on the factor V metalloprotein.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Hematology

    Background:

    • Coagulation factor V (FV) is a crucial protein in the prothrombinase complex.
    • Unlike coagulation factor Xa, FV binds phospholipids independently of Ca2+.
    • The role of calcium in FV's structure and function requires further investigation.

    Purpose of the Study:

    • To investigate the presence and role of calcium within the factor V molecule.
    • To understand the interaction between factor V, calcium, and phospholipids.

    Main Methods:

    • Enzyme activity assays using various calcium chelators (oxalate, citrate, pyrophosphate, EDTA).
    • Investigating the effects of divalent cations (Ca2+, Mn2+, Mg2+) on FV activity.
    • Assessing the impact of urea denaturation and phospholipid binding on calcium association.

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    Main Results:

    • Chelator-induced inhibition of FV activity was time- and concentration-dependent, correlating with chelator-calcium association constants.
    • Inhibition was prevented by Ca2+ and Mn2+, but not Mg2+, and could be reversed under specific conditions.
    • FV contains approximately 1 g atom of calcium per 300,000 daltons, which is not removed by EDTA under native conditions.
    • EDTA removed >80% of calcium in 8 M urea, and phospholipid pre-binding prevented EDTA inhibition.

    Conclusions:

    • Factor V is a calcium-binding metalloprotein.
    • Phospholipids appear to complex at the calcium-binding site on factor V.
    • The native structure of factor V is essential for maintaining its calcium-binding site.