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Comparison of angiotensin II and SAR1, Ile8-AII binding to solubilized receptors in the bovine adrenal

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6936252

Derivatives of angiotensin with a sarcosine substitution at the carboxy terminus and an aliphatic amino acid substitution at the amino terminus have been shown to be competitive ligands for the angiotensin receptor. Scatchard plots derived from saturation isotherm data in bovine adrenal particulates consistently demonstrate three to five times the number of binding sites for /sup 125/I-Sarl,Ile8-AII (/sup 125/I-SI-AII) than for /sup 125/I-AII in experiments in which the two ligands are run side-by-side. A significant difference between /sup 125/I-AII and /sup 125/I-SI-AII binding to detergent solubilized angiotensin receptors was observed. Of the /sup 125/I-AII binding sites, about 85-90% were recovered upon solubilization. In contrast, the recovery of /sup 125/I-SI-AII binding sites was only 4-5%. To determine whether binding sites labeled in the soluble state represent biologically significant AII receptors, they examined the ability of selected angiotensin analogs to inhibit /sup 125/I-AII binding and /sup 125/I-SI-AII binding. Synthetic analogs of angiotensin effectively competed with /sup 125/I-AII for the binding sites with a relative potency of AIII > AII > AI > SI-AII. When /sup 125/I-SI-AII was used as a main ligand the relative potency of the synthetic analogs for the binding site was SI-AII > AII > AIII > AI. One possible explanation for the above is that /sup 125/I-AII and /sup 125/I-SI-AII are binding to separate sites.

Research Organization:
Washington State Univ., Pullman
OSTI ID:
6936252
Report Number(s):
CONF-8604222-
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Vol. 45:4; ISSN FEPRA
Country of Publication:
United States
Language:
English