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- W2006870147 abstract "1.1. Several biochemical properties of adenylate cyclase were examined in particulate and detergent-solubilized preparations of gill tissue in Aplysia californica.2.2. Enzyme activity in a 38,000 g particulate fraction was stimulated 250-fold by NaF and 23-fold by guanyl-5′-yl-imidodiphosphate. Stimulation of activity by dopamine and 5-hydroxytryptamine displayed an absolute requirement for guanine nucleotide.3.3. Enzyme activity was supported by both Mg2+ and Mn2+, activity being 8-fold greater in the presence of saturating concentrations of the latter cation.4.4. Solubilization of the enzyme with nonionic detergents caused a loss in sensitivity to guanyl-5′-yl-imidodiphosphate while NaF stimulation was enhanced.5.5. In the presence of calmodulin, Ca2+ augmented basal as well as dopamine- and serotonin-stimulated activity at concentrations below 10 μM; concentrations above this were inhibitory.6.6. The diterpene forskolin had no stimulatory action on either the membrane-bound or detergent-solubilized enzyme.7.7. The data show that neurohormone-sensitive adenylate cyclase in this invertebrate tissue resembles, in many respects, the enzyme from mammalian tissues." @default.
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- W2006870147 date "1985-01-01" @default.
- W2006870147 modified "2023-09-27" @default.
- W2006870147 title "Biochemical properties of adenylate cyclase in the gill of Aplysia californica" @default.
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- W2006870147 doi "https://doi.org/10.1016/0305-0491(85)90205-6" @default.
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