Homologous somatotropin radioreceptor assay utilizing recombinant bovine growth hormone

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

Research output: Contribution to journalArticle

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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