Covalent coupling of bovine growth hormone to its receptor in bovine liver membranes

Lokenga Badinga, Robert J. Collier, William W. Thatcher, Sergio J. Quintana, Fuller W. Bazer

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


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 languageEnglish (US)
Pages (from-to)85-89
Number of pages5
JournalMolecular and Cellular Endocrinology
Issue number1-2
StatePublished - Jul 1987
Externally publishedYes


  • Bovine growth hormone
  • Cross-linking
  • Somatotropin receptor

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Endocrinology


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