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Related Experiment Videos

Subunit structure of 27 S thyroid iodoprotein.

O Tarutani, T Kondo, D J Smith

    Endocrinologia Japonica
    |August 1, 1976
    PubMed
    Summary

    Thyroid 27 S iodoprotein dissociates into subunits when treated with sodium dodecyl sulfate (SDS) or succinic anhydride. This iodoprotein, composed of thyroglobulin molecules, exhibits greater resistance to dissociation than thyroglobulin itself.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Endocrinology

    Background:

    • Thyroid iodoprotein is crucial for thyroid hormone synthesis.
    • Understanding its structure and dissociation is key to thyroid function.
    • Previous hypotheses suggested 27 S iodoprotein is a dimer of thyroglobulin.

    Purpose of the Study:

    • To investigate the dissociation patterns of thyroid 27 S iodoprotein.
    • To compare its dissociation with thyroglobulin.
    • To analyze its subunit composition and chemical characteristics.

    Main Methods:

    • Ultracentrifugation
    • Polyacrylamide gel electrophoresis
    • Sodium dodecyl sulfate (SDS) treatment
    • Succinic anhydride treatment

    Main Results:

    • SDS and succinic anhydride treatment dissociated 27 S iodoprotein into three subunits (S-19, S-17, S-12).
    • The S-12 subunit was predominant at higher SDS concentrations.
    • Dissociation products were qualitatively similar to thyroglobulin, supporting the thyroglobulin dimer hypothesis.
    • 27 S iodoprotein showed higher resistance to dissociation than thyroglobulin.
    • Chemical composition (sialic acid, hexose, iodoamino acids) was comparable to thyroglobulin.

    Conclusions:

    • Thyroid 27 S iodoprotein is composed of two thyroglobulin molecules.
    • It possesses a distinct subunit structure conferring greater stability than thyroglobulin.
    • Its chemical composition is similar to thyroglobulin, with minor variations.

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