Abstract
High-affinity forskolin binding sites in brain membranes have been identified that have structure-activity characteristics compatible with forskolin's site of action at the adenylate cyclase enzyme. It is proposed that these high-affinity binding sites are associated with an activated complex of the catalytic protein and the alpha s subunit. Quantitation of high-affinity forskolin binding sites may provide a direct measure of the amount of adenylate cyclase that has the potential to be regulated by stimulatory hormones and the Ns subunit.
MeSH terms
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Adenylyl Cyclases / metabolism*
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Animals
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Brain / metabolism*
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Cations, Divalent / pharmacology
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Colforsin
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Diterpenes / metabolism*
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Edetic Acid / pharmacology
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Enzyme Activation
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Fluorides / pharmacology
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GTP-Binding Proteins / metabolism
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Guanylyl Imidodiphosphate / pharmacology
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Kinetics
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Protein Binding / drug effects
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Rats
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Structure-Activity Relationship
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Synaptosomes / metabolism
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Temperature
Substances
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Cations, Divalent
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Diterpenes
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Colforsin
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Guanylyl Imidodiphosphate
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Edetic Acid
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GTP-Binding Proteins
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Adenylyl Cyclases
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Fluorides