High-affinity binding of forskolin to rat brain membranes.
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.
Seamon
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Daly
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JW
D000262:Adenylyl Cyclases / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000378:metabolism*; D002413:Cations, Divalent / Q000494:pharmacology; D005576:Colforsin; D004224:Diterpenes / Q000378:metabolism*; D004492:Edetic Acid / Q000494:pharmacology; D004789:Enzyme Activation; D005459:Fluorides / Q000494:pharmacology; D019204:GTP-Binding Proteins / Q000378:metabolism; D006165:Guanylyl Imidodiphosphate / Q000494:pharmacology; D007700:Kinetics; D011485:Protein Binding / Q000187:drug effects; D051381:Rats; D013329:Structure-Activity Relationship; D013574:Synaptosomes / Q000378:metabolism; D013696:Temperature
D002413:Cations, Divalent; D004224:Diterpenes; D005576:Colforsin; D006165:Guanylyl Imidodiphosphate; D004492:Edetic Acid; D019204:GTP-Binding Proteins; D000262:Adenylyl Cyclases; D005459:Fluorides