Binding of serotonin to soluble protein from synaptosomes.

作者: Hadassah Tamir , Yung-yu L. Huang

DOI: 10.1016/0024-3205(74)90248-3

关键词: CytosolDissociation constantReserpineTryptamineSerotoninBiochemistryChemistryTryptophanRaphe nucleiBinding protein

摘要: Abstract A soluble protein with high binding affinity for serotonin was detected in synaptosomes and cytosol of cortex stem rat brain. Both dopamine inhibited the labeled serotonin. 5, 7-dihydroxytryptamine a very effective inhibitor whereas other indole derivatives, such as tryptamine, 5-HIAA, N-w-methyl serotonin, tryptophan did not inhibit binding. Sulfhydryl-blocking reagents Ca++ also The serotonin-protein complex, which has dissociation constant 10−8 M, could be separated from bulk by gel electrophoresis. Studies distribution different regions brain showed that hypothalamus region raphe nuclei have higher capacity than either cortex, cerebellum, or white matter. Binding fraction increased several fold after administration p-chlorophenylalanine reserpine to animals.

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