Abstract
The function of sodium dependent neurotransmitter transport is probably to terminate the overall process of synaptic transmission. Recent studies have shown that in these transport systems, such as those for?-aminobutyric acid (GABA), glutamate and biogenic amines, solute fluxes are not only coupled to sodium but also to additional ions. The GABA transporter, for instance, appears to catalyze electrogenic cotransport of GABA, sodium and chloride. The glutamate transporter catalyses electrogenic cotransport of sodium and glutamate while potassium is antiported. The role of potassium in the translocation cycle is to allow the return of the “unloaded transporter”. The glutamate as well as the GABA transporter have been solubilised from plasma membranes deriveed from rat brain and reconstituted into liposomes. The resulting proteolipo-somes exhibited glutamate and GABA transport with the same characteristics as in the native vesicles. The GABA transporter has been purified to near homogeneity using transport activity upon reconstitution as an assay. Purification steps included fractionation of the cholate extract with ammonium sulfate, DEAE cellulose and lectin-chromatography. It appears that the GABA transporter is a glycoprotein with a molecular weight of 82–85 KDa. (Supported by NIH grant NS 16708).
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Kanner, B.I., Radian, R. (1986). Mechanisms of Reuptake of Neurotransmitters from the Synaptic Cleft. In: Roberts, P.J., Storm-Mathisen, J., Bradford, H.F. (eds) Excitatory Amino Acids. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-08479-1_11
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