Horm Metab Res 1988; 20(5): 278-281
DOI: 10.1055/s-2007-1010815
ORIGINALS

© Georg Thieme Verlag, Stuttgart · New York

Human Growth Hormone Binds to Lactogenic Receptors in Bovine, Ovine and Rat Adrenals

L.-C. Teh, C. J. Ormandy, A. S. Surus, R. L. Sutherland, G. E. Chapman
  • Garvan Institute of Medical Research, St. Vincent's Hospital, Darlinghurst, NSW, Australia
Weitere Informationen

Publikationsverlauf

1986

1987

Publikationsdatum:
14. März 2008 (online)

Summary

The distribution of 125I radioactivity in the liver, kidneys, adrenals and serum of male rats was measured 10 minutes after an intravenous bolus of 125I-labelled human growth hormone (hGH) was administered in the presence or absence of a large excess of ovine growth hormone or ovine prolactin. The hGH binding sites in the adrenals had displacement properties characteristic of lactogenic receptors, whereas those in the liver had displacement properties characteristic of somatogenic receptors. Bovine and ovine adrenal microsomal membrane fractions contained high affinity (Ka = 1.4-3.3 nM-1) binding sites for hGH which showed ligand specificity typical of lactogenic receptors. It is concluded that the hGH binding site in the adrenal gland is a classical lactogenic receptor and that this tissue is a convenient and rich (42.6±6.4 fmol hGH specifically bound/mg protein) source of receptor suitable for further characterization.