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Subunit structure of 27 S thyroid iodoprotein

O Tarutani, T Kondo, D J Smith

    Endocrinologia Japonica
    |August 1, 1977
    PubMed
    Summary

    Thyroid 27 S iodoprotein dissociates into subunits with sodium dodecyl sulfate (SDS) or succinic anhydride. This iodoprotein shows greater resistance to dissociation than thyroglobulin, despite similar chemical composition.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Endocrinology

    Background:

    • Thyroid 27 S iodoprotein is a key component involved in thyroid hormone synthesis.
    • Understanding its structure and dissociation is crucial for comprehending thyroid function.

    Purpose of the Study:

    • To investigate the dissociation patterns of thyroid 27 S iodoprotein using sodium dodecyl sulfate (SDS) and succinic anhydride.
    • To compare the dissociation products and resistance of 27 S iodoprotein with thyroglobulin.

    Main Methods:

    • Ultracentrifugation
    • Polyacrylamide gel electrophoresis
    • SDS-PAGE
    • Succinylation

    Main Results:

    • SDS treatment dissociated 27 S iodoprotein into three subunits (S-19, S-17, S-12), with S-12 predominating at higher SDS concentrations.
    • Succinylation yielded similar dissociation patterns to SDS treatment.
    • Dissociation products were qualitatively similar to thyroglobulin, supporting the hypothesis that 27 S iodoprotein consists of two thyroglobulin molecules.
    • 27 S iodoprotein exhibited higher resistance to dissociation compared to thyroglobulin.
    • Chemical composition (sialic acid, hexose, iodoamino acids) of 27 S iodoprotein was comparable to thyroglobulin.

    Conclusions:

    • Thyroid 27 S iodoprotein is composed of two thyroglobulin molecules with a distinct subunit structure.
    • The protein demonstrates increased resistance to dissociation agents, suggesting structural differences from thyroglobulin.
    • Further studies on subunit interactions and chemical composition are warranted.

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