Serotonin uptake, binding and release were studied in human blood platelets. The uptake showed marked individual differences while the loss of 5-HT during resuspension of the 5-HT loaded platelets was constant. The existence of 5-HT binding proteins was demonstrated by equilibrium dialysis, gel filtration on a column equilibrated with 5-HT, affinity chromatography on a 5-HT-Sepharose column and polyacryl-amide disc gel electrophoresis experiments. After incubation of the platelet extract in the presence of [14-C]5-HT, electrophoretic and autoradiographic analysis demonstrated the presence of three 5-HT binding proteins, two of which were soluble glycoproteins specific for serotonin.
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