Homologous somatotropin radioreceptor assay utilizing recombinant bovine growth hormone

Luis S. Haro, Robert J. Collier, Frank J. Talamantes

    Research output: Contribution to journalArticlepeer-review

    33 Scopus citations

    Abstract

    A homologous radioreceptor assay using recombinant bovine growth hormone and bovine liver membranes is described. The total specific binding of 125I-labeled recombinant bovine growth hormone to the 100000 × g pellet was 48% in 24 h at 25 °C. Hormone binding was partially reversible, with 40% of the radiolabeled hormone being irreversibly bound. The amount of specific binding varied with assay pH, with the optimum occurring at pH 7.8. Specific binding was temperature-dependent, with greater specific binding occurring at 25°C than at 5°C or 37°C during a 24 h period. Recombinant bovine growth hormone, human growth hormone, ovine growth hormone and recombinant porcine growth hormone competed effectively with 125I-labeled recombinant bovine growth hormone for binding sites, while bovine prolactin and ovine prolactin were needed in amounts 106-fold the concentration of recombinant bovine growth hormone to displace the radiolabeled hormone. Surprisingly, human placental lactogen did not displace the radiolabeled hormone.

    Original languageEnglish (US)
    Pages (from-to)109-116
    Number of pages8
    JournalMolecular and Cellular Endocrinology
    Volume38
    Issue number2-3
    DOIs
    StatePublished - Dec 1984

    Keywords

    • bovine growth hormone
    • growth hormone receptor
    • homologous hormone-receptor system
    • radioreceptor assay
    • somatogenic

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Endocrinology

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