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 language | English (US) |
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Pages (from-to) | 109-116 |
Number of pages | 8 |
Journal | Molecular and Cellular Endocrinology |
Volume | 38 |
Issue number | 2-3 |
DOIs | |
State | Published - Dec 1984 |
Keywords
- bovine growth hormone
- growth hormone receptor
- homologous hormone-receptor system
- radioreceptor assay
- somatogenic
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Endocrinology