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- W1970434202 abstract "A soluble protein with high binding affinity for serotonin was detected in synaptosomes and cytosol of cortex and stem of rat brain. Both serotonin and dopamine inhibited the binding of labeled serotonin. 5, 7-dihydroxytryptamine was a very effective inhibitor whereas other indole derivatives, such as tryptamine, 5-HIAA, N-w-methyl serotonin, and tryptophan did not inhibit the binding. Sulfhydryl-blocking reagents and Ca++ also inhibited the binding. The serotonin-protein complex, which has a dissociation constant of 10−8 M, could be separated from the bulk of the soluble protein by gel electrophoresis. Studies of the distribution of binding protein in different regions of brain showed that hypothalamus and the region of raphe nuclei have a higher binding capacity than either cortex, cerebellum, or white matter. Binding capacity of the soluble protein fraction of brain stem increased several fold after administration of p-chlorophenylalanine or reserpine to the animals." @default.
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- W1970434202 date "1974-01-01" @default.
- W1970434202 modified "2023-09-27" @default.
- W1970434202 title "Binding of serotonin to soluble protein from synaptosomes" @default.
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- W1970434202 doi "https://doi.org/10.1016/0024-3205(74)90248-3" @default.
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