title: Endogenous components of the striatum confer dopamine-sensitivity upon adenylate cyclase activity: the role of endogenous guanyl nucleotides.
abstract: Repeated washing of the particulate material from rat striatum abolishes the dopamine-sensitivity of the adenylate cyclase activity. Readdition of the soluble fraction of the caudate homogenate restores the dopamine-sensitivity to the enzyme activity. Fractions, prepared with thin layer chromatography, containing endogenous GTP and GDP also restore dopamine-sensitivity to striatal adenylate cyclase activity. The effectiveness of GDP results from its conversion to GTP during the assay; when this conversion is eliminated, GDP can specifically block the coupling between the dopamine receptor and adenylate cyclase.
mesh_terms: D000262:Adenylyl Cyclases / Q000378:metabolism*; D000266:Adenylyl Imidodiphosphate / Q000378:metabolism; D000818:Animals; D002421:Caudate Nucleus / Q000201:enzymology; D003342:Corpus Striatum / Q000201:enzymology*; D004298:Dopamine / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D006150:Guanine Nucleotides / Q000502:physiology*; D006153:Guanosine Diphosphate / Q000302:isolation & purification / Q000502:physiology*; D006160:Guanosine Triphosphate / Q000302:isolation & purification / Q000502:physiology*; D008297:Male; D051381:Rats; D011954:Receptors, Dopamine / Q000502:physiology
chemical_list: D006150:Guanine Nucleotides; D011954:Receptors, Dopamine; D006153:Guanosine Diphosphate; D000266:Adenylyl Imidodiphosphate; D006160:Guanosine Triphosphate; D000262:Adenylyl Cyclases; D004298:Dopamine