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Filter-binding assay procedure for thyroid hormone receptors.

A Inoue, J Yamakawa, M Yukioka

    Analytical Biochemistry
    |October 1, 1983
    PubMed
    Summary
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    A new filter-binding assay accurately measures thyroid hormone receptor activity. This method simplifies thyroid hormone receptor (THR) analysis, offering a reliable alternative to traditional techniques for routine laboratory use.

    Area of Science:

    • Endocrinology
    • Molecular Biology
    • Biochemistry

    Background:

    • Thyroid hormones regulate crucial physiological processes.
    • Accurate measurement of thyroid hormone receptor (THR) activity is essential for understanding hormone action.
    • Existing methods for THR assessment can be complex and time-consuming.

    Purpose of the Study:

    • To develop a simplified and accurate assay for measuring thyroid hormone receptor (THR) activity.
    • To establish a reliable filter-binding method for routine laboratory applications.

    Main Methods:

    • Extraction of THR from rat liver nuclei using a 0.4 M NaCl solution.
    • Incubation of extracted receptors with 125I-labeled triiodothyronine (T3).
    • Filtration of the reaction mixture through cellulose ester membranes followed by radioactivity counting.

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    Main Results:

    • The developed filter-binding assay demonstrated a linear relationship between receptor activity and protein concentration.
    • Comparison with the conventional Sephadex G-25 column method showed the filter-binding assay's effectiveness.
    • Optimization of filtration conditions led to a standardized assay procedure.
    • The assay determined an apparent dissociation constant (Kd) of 1.38 X 10(-10) M for THR and a pH optimum of 8.2-8.4 for T3 binding.

    Conclusions:

    • The nitrocellulose membrane filter-binding assay provides an accurate and efficient method for quantifying thyroid hormone receptor (THR) activity.
    • This technique is suitable for routine assays, offering a practical alternative to existing methods.
    • The established procedure facilitates reliable assessment of THR binding characteristics.