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Coagulation Factor V contains copper ion.

K G Mann, C M Lawler, G A Vehar

    The Journal of Biological Chemistry
    |November 10, 1984
    PubMed
    Summary

    Bovine and human coagulation Factor V contain bound copper. Unlike ceruloplasmin, Factor V does not show specific spectral properties or oxidase activity, suggesting distinct copper binding.

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    Area of Science:

    • Biochemistry
    • Hematology
    • Protein Chemistry

    Background:

    • Coagulation Factor V is essential for blood clotting.
    • Ceruloplasmin is a copper-binding protein involved in iron metabolism and possesses oxidase activity.
    • Sequence homology suggests potential functional similarities between Factor V and ceruloplasmin.

    Purpose of the Study:

    • To investigate the presence and nature of copper binding in coagulation Factor V.
    • To compare the copper binding site and oxidase activity of Factor V with that of ceruloplasmin.

    Main Methods:

    • Atomic absorption and atomic emission spectroscopy were used to quantify copper in Factor V preparations.
    • Visible and near-ultraviolet absorption spectroscopy assessed spectral properties of Factor V and Factor Va.
    • Enzyme kinetics measured the ability of Factor V and Factor Va to oxidize N,N-dimethyl-p-phenylenediamine.

    Main Results:

    • Bovine and human Factor V preparations consistently contained copper at a 1:1 molar ratio (copper:Factor V).
    • Factor V and activated Factor Va (Factor Va) lacked the characteristic spectral maxima (310 or 610 nm) found in ceruloplasmin.
    • Factor V and Factor Va did not exhibit oxidase activity towards N,N-dimethyl-p-phenylenediamine under optimal conditions for ceruloplasmin.

    Conclusions:

    • Coagulation Factor V binds copper ions.
    • The copper binding site in Factor V appears functionally and structurally distinct from the copper sites in ceruloplasmin.
    • Factor V's copper ion likely plays a role independent of ceruloplasmin's oxidase function.

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