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Isolation and characterization of hog thyroid actin.

F Martin

    Comparative Biochemistry and Physiology. B, Comparative Biochemistry
    |January 1, 1984
    PubMed
    Summary

    Hog thyroid glands contain actin, a key protein. Researchers isolated and purified this actin, finding it forms filaments under specific conditions, crucial for understanding muscle and cell structure.

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Endocrinology

    Background:

    • Actin is a crucial protein involved in muscle contraction and cell structure.
    • Thyroid glands are primarily known for hormone production, but their protein composition is less explored.

    Purpose of the Study:

    • To isolate and characterize actin from hog thyroid glands.
    • To determine the properties and polymerization behavior of thyroid actin.

    Main Methods:

    • Protein isolation from acetone-dehydrated hog thyroid slices.
    • Purification using gel filtration and DEAE-cellulose chromatography.
    • Two polymerization-depolymerization cycles for actin purification.

    Main Results:

    • Actin constitutes approximately 4.6% of hog thyroid protein, excluding thyroglobulin.
    • Purified actin (Mr = 42000) comprises beta and gamma species in a 2:1 ratio.
    • Thyroid actin polymerized into 6 nm filaments under specific ionic conditions (0.1 M KCl, 2 mM MgCl2), with a critical concentration of 30 µg/ml and intrinsic viscosity of 4.7 dl/g.

    Conclusions:

    • Hog thyroid glands are a source of purified actin.
    • Thyroid actin exhibits polymerization characteristics similar to other non-muscle actins.
    • This study provides insights into the non-hormonal protein components of the thyroid gland.

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