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- W1968625139 abstract "Abstract We have investigated the substrate specificity of thyroid adenyl cyclase using sheep thyroid homogenates. The basal conversion of ATP [0.1 mM] to 3′, 5′-AMP by this enzyme was found to be markedly inhibited [82%] by 1 mM deoxyATP [dATP], reduced by 1 mM TTP [33%] and UTP [30%] but was unaffected by 1 mM CTP, GTP or ITP. TSH- and sodium fluoride-induced enzyme activation showed a similar response [dATP inhibition 91% and 83%, respectively], although in contrast to basal and TSH cyclase activation all other triphosphates tested reduced fluoride activation by 17 to 31%. When concentration of added triphosphates was reduced to 0.1 mM, however, only dATP reduced basal and stimulated cyclase activity. Thyroid homogenate converted [α- 32 P] dATP to [ 32 P] 3′, 5′-dAMP and this conversion was augmented 3-to-4 fold by TSH and NaF. Basal and stimulated 3′, 5′-dAMP formation from dATP [0.1 mM] was inhibited [49% to 62%] by 1 mM ATP but was not modified by any of the other triphosphates. Demonstration that 3′, 5′-AMP formation is inhibited by dATP while 3′, 5′-dAMP formation is inhibited by ATP, together with the findings that TSH and NaF stimulate the formation of 3′, 5′-dAMP as well as 3′, 5′-AMP, suggest that the thyroid adenyl cyclase enzyme is base-specific and utilizes both ATP and dATP as substrates." @default.
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- W1968625139 date "1970-07-01" @default.
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- W1968625139 title "Substrate specificity of thyroid adenyl cyclase" @default.
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- W1968625139 doi "https://doi.org/10.1016/0024-3205(70)90334-6" @default.
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