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Insulin receptor isolation studies

F M Finn, G Titus, H Nemoto

    Metabolism: Clinical and Experimental
    |July 1, 1982
    PubMed
    Summary
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    Researchers developed a biospecific affinity method using biotinylated insulin to purify insulin receptors. This technique successfully isolates insulin receptors from human placenta, offering a scalable purification approach.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Affinity Chromatography

    Background:

    • Insulin receptor purification is crucial for understanding its function.
    • Existing methods face challenges with receptor stability and contamination.
    • Biotin-avidin binding offers a specific interaction for affinity purification.

    Purpose of the Study:

    • To develop and validate a biospecific affinity chromatography method for insulin receptor purification.
    • To assess the applicability of this method for preparative scale purification.
    • To characterize contaminants and evaluate analytical methods for their detection.

    Main Methods:

    • Utilized N alpha,B1-biotinylinsulin immobilized on succinylavidin-AH Sepharose 4B.
    • Employed noncovalent attachment of biotinylated insulin for receptor binding.

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  • Applied 20 mM biotin elution for receptor recovery and HPLC for enzyme activity assessment.

    • Main Results:

    • Successfully bound and eluted solubilized human placental insulin receptor using the biotinylated insulin affinity resin.
    • Isolated a high molecular weight fraction containing the insulin receptor, confirmed by antibody cross-reactivity.
    • Identified and quantified "insulinase" contamination using HPLC, demonstrating its inhibition by N-ethylmaleimide.

    Conclusions:

    • The developed biospecific affinity technique is effective for purifying insulin receptors.
    • This method shows promise for preparative scale isolation of functional insulin receptors.
    • HPLC offers a sensitive tool for assessing "insulinase" activity in receptor preparations.