Abstract

The cDNA chimeras between two subtypes of mouse excitatory amino acid transporter family, mouse excitatory amino acid carrier 1 (mEAAC1) and mouse alanine serine cysteine transporter 1 (mASCT1), were constructed by recombinant PCR. After transcriptionin vitro, the cRNA was injected and expressed inXenopus laevis oocytes.3H-Glu and3H-Ser were used as isotopic tracer to measure the flux of amino acids. The results showed that there might not be the key amino acids responsible for substractive specificity in the NH2-terminal and its adjacent regions of these two transporters, which probably supported the formation of the substrate binding sites.

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