Abstract
Angiotensin binding and the effects of angiotensin on adenylate cyclase activity were determined on purified membranes from the glomerulosa zone of bovine adrenal cortex. Angiotensin II inhibited adenylate cyclase activity in a dose-dependent manner with an A 50-value of 2 nM. The angiotension effect required the presence of GTP. Angiotensin also inhibited ACTH-stimulated activity. Angiotensin binding was sensitive to the same effectors which influenced angiotensin-induced adenylate cyclase inhibition. In the presence of NaCl 100 mM and magnesium, angiotensin interacted with a single population of binding sites (K d = 4 nM and maximal binding capacity of 440 fmol/mg protein). These results and published data suggest that the ability to inhibit adenylate cyclase might be a general property of angiotensin receptors.