Rationale: In the paper the isolation of the EAAT5, an excitatory amino acid transporter is described. In figure 3 the uptake of 3H-L-glutamate and 3H-L-Aspertate are demonstrated in oocytes injected with the EAAT5 mRNA and voltage-clamped at −60 mV. In comparison to controls (uninjected oocytes), the uptake was typically 2- to 10-fold larger. The uptake is sodium- and voltage-dependent. These data indicate that the transporter functions as a glutamate transporter. Table 1 summarizes specificity and kinetic values of the transporter.. Experimental description: The isolation of an EAAT subtype from salamander retina whose sequence differed substantially from previously reported mammalian sequences lead us to isolate the human homolog EAAT5.