Initial characterization and sexual dimorphism of serum growth hormone-binding protein in adult rats.

@article{Massa1990InitialCA,
  title={Initial characterization and sexual dimorphism of serum growth hormone-binding protein in adult rats.},
  author={Giulio Massa and Noordin Mulumba and Jean Marie Ketelslegers and Marc Maes},
  journal={Endocrinology},
  year={1990},
  volume={126 4},
  pages={1976-80}
}
The in vitro binding of 125I-bovine growth hormone (bGH) to adult rat serum was studied using Ultrogel AcA34 filtration. When analytical chromatography on a 1.6 x 100 cm column was performed, four peaks of radioactivity were revealed: the first two peaks with Mr +/- 220,000 and +/- 110,000 corresponded to bound 125I-bGH (abolished by excess of unlabeled bGH), the third corresponded to free 125I-bGH and the fourth to free Na125I (Vt). On a short (1 x 40 cm) column, bound 125I-bGH eluted as a… CONTINUE READING