Abstract
The structure of bovine somatotropin receptor was examined following covalent coupling of iodinated recombinant bovine growth hormone ([125I]rbGH) to bovine liver membrane receptors using ethylene glycol bis(succinimidyl succinate). Iodinated rbGH was incorporated into a complex of estimated Mr of 140000 under reducing conditions. Excess unlabeled rbGH, but not bovine prolactin (bPRL), inhibited completely the incorporation of [125I]rbGH into the Mr = 140000 species. In dairy bulls, the Mr = 140000 complex was undetectable soon after birth but became predominant at 6 months of age. No evidence was found to support presence of bPRL receptors in steer liver membranes. Assuming a 1:1 stoichiometry of hormone binding to receptor, it appears that bGH binds to a major receptor subunit of Mr = 119000 which does not recognize bPRL.
Original language | English (US) |
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Pages (from-to) | 85-89 |
Number of pages | 5 |
Journal | Molecular and Cellular Endocrinology |
Volume | 52 |
Issue number | 1-2 |
DOIs | |
State | Published - Jul 1987 |
Externally published | Yes |
Keywords
- Bovine growth hormone
- Cross-linking
- Somatotropin receptor
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Endocrinology