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Human thyrotropin and its alpha and beta subunits

J Closset, G Hennen, R M Lequin

    Archives Internationales De Physiologie Et De Biochimie
    |December 1, 1977
    PubMed
    Summary
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    Researchers developed a new method to isolate human thyrotropin (hTSH) and its subunits using chromatography. The purified hTSH showed significant thyroid stimulating activity, and subunit characterization revealed distinct amino-terminal residues and chain lengths.

    Area of Science:

    • Biochemistry
    • Endocrinology
    • Protein Chemistry

    Background:

    • Human thyrotropin (hTSH) is crucial for thyroid hormone regulation.
    • Previous methods for hTSH isolation and subunit separation were complex.
    • Characterization of hTSH subunits is essential for understanding hormone function.

    Purpose of the Study:

    • To describe a novel, simplified procedure for isolating intact human thyrotropin.
    • To develop a new method for obtaining purified alpha and beta subunits of human thyrotropin.
    • To characterize the isolated subunits, including amino-terminal residues and potential structural differences.

    Main Methods:

    • Isolation of intact human thyrotropin using ion exchange chromatography and gel filtration.
    • Separation of alpha and beta subunits via incubation in acidified 8 M urea followed by chromatography.

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  • Quantification of thyroid stimulating activity using bioassay.
  • Measurement of subunit cross-contamination using radioimmunoassay.

    • Main Results:

    • A new isolation procedure for human thyrotropin was successfully established.
    • The purified human thyrotropin preparation exhibited a thyroid stimulating activity of 0.5 IU/mg.
    • The alpha and beta subunits were isolated, with valine and phenylalanine as amino-terminal residues, respectively.
    • The beta subunit was found to be shorter than its bovine counterpart by one methionine residue.
    • Radioimmunoassay indicated minimal cross-contamination between the isolated alpha and beta subunits.

    Conclusions:

    • The described methods provide an efficient means for obtaining purified human thyrotropin and its subunits.
    • The characterization data contribute to the understanding of human thyrotropin structure and function.
    • This work offers a valuable resource for further research in thyroid endocrinology.