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Related Experiment Videos

67 kDa calcimedin, a new Ca2+-binding protein.

P B Moore

    The Biochemical Journal
    |August 15, 1986
    PubMed
    Summary

    Researchers identified four calcimedins in muscle tissue. The 67 kDa calcimedin was purified and characterized as a novel calcium-binding protein distinct from others known.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Muscle Physiology

    Background:

    • Calcimedins are proteins found in various muscle types.
    • Previous studies indicated the presence of four calcimedins with different molecular weights.

    Purpose of the Study:

    • To purify and characterize the 67 kDa calcimedin.
    • To determine if the 67 kDa calcimedin is a novel calcium-binding protein.

    Main Methods:

    • Fluphenazine-Sepharose affinity chromatography for initial isolation.
    • DEAE-cellulose chromatography and phenyl-Sepharose chromatography for purification.
    • SDS-PAGE for molecular weight determination.
    • Amino acid analysis and circular dichroism (c.d.) for structural characterization.
    • Calcium-binding studies to determine binding affinity.

    Main Results:

    • Four calcimedins were isolated from smooth, cardiac, and skeletal muscle.
    • The 67 kDa calcimedin was purified to homogeneity.
    • Amino acid analysis revealed no trimethyl-lysine and 2 mol of tryptophan per mole of protein.
    • Circular dichroism indicated positive ellipticity in the near-UV range.
    • Calcium-binding studies showed one high-affinity Ca2+-binding site (Kd = 0.4 microM).

    Conclusions:

    • The 67 kDa calcimedin is a distinct protein.
    • It possesses a high-affinity calcium-binding site.
    • This protein is different from other known calcium-binding proteins.

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