{'fraction_non_alphanumeric': 0.020251396648044692, 'fraction_numerical': 0.019553072625698324, 'mean_word_length': 5.312775330396476, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Studies on inhibition of angiotensin II receptors in rabbit adrenal and aorta.

Angiotensin II (AII) labeled with 125I binds to rabbit adrenal cortical membranes over a concentration range from 0.5 to 20 nM at an apparent single site with a KD of 5 nM. This binding was inhibited in a surmountable fashion with respect to AII by the peptide analogs sarcosine1 (Sar1),Leu8AII and Phe4, Tyr8 AII when added to the incubation media concomitant with AII addition. With a 30-min preincubation, however, the former inhibitor displayed nonsurmountable kinetics whereas the profile of the latter was unaffected. In rabbit aortic strips with the same preincubation time, the Sar1Leu8AII analog was a nonsurmountable antagonist of the contractile effect of AII whereas the inhibition produced by Phe4,Tyr8AII was surmountable by increasing agonist (AII) concentrations. The inhibitory effect of the former was maintained after repeated washing of the tissue whereas that of the latter was readily reversible. Addition of Phe4,Tyr8AII to the bath 5 min before preincubation protected the tissue from the prolonged AII inhibition by Sar1,Leu8AII. These findings indicate different kinetic modes of AII inhibition by these two antagonists. Phe4,Tyr8AII behaves as a reversible, competitive inhibitor of AII binding, whereas Sar1,Leu8AII combines with the AII receptor in a slowly dissociable manner and is therefore not readily displaced by AII.