The characterisation of two partially purified systems for Na+-dependent amino acid transport

Two systems mediating the transport of amino acids were studied in vesicles derived from protein-depleted membranes of pigeon erythrocytes. One system (ASC system) catalysed the Na+-dependent exchange of small neutral amino acids, such as alanine, serine and cysteine. The other system, also Na+-dependent, mediated the active transport of glycine. The ASC and glycine systems were distinguished by the sensitivity of the latter to the anion present, by the former's requirement for an exchangeable amino acid and by the inability of alanine to inhibit the transport of glycine. Preliminary results indicated that the influx of glycine was electrically silent. The only major integral protein retained in the vesicles was the band 3 protein, but that could not be unequivocally identified as the transporter.