Abstract
The adenyl cyclase activity of rat erythrocyte ghosts was found to be activated by sodium fluoride, catecholamines, and prostraglandin E2, but not by a large numer of hormones active in other systems. The enzyme activation was of mixed alpha and beta types, in that the response to norepinephrine was a) much weaker than that to isoproterenol b) blocked by the beta-blocking agents dichloroisoproterenol ad propranolol and c) inhibited by the alpha-blocking agents phentolamine and phenoxybenzamine, as well as by serotonin. The activity of a theophylline-sensitive adenosine cyclic 3',5'-phosphate phosphodiesterase was found in the erythrocytes of several species. The order of activities was the following: mouse > rat > cat = dog > human. Less than 10% of the cyclic 3', 5'-AMP phosphodiesterase activity appeared to be membrane-bound and, like the soluble form, it was markedly inhibited by theophylline.
- Copyright ©, 1970, by Academic Press Inc.
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