Do neutral amino acids and their N-methylated analogues share the same Na-dependent carrier in brush-border membrane from the eel intestine?

• Published in: Comparative Biochemistry and Physiology Part A: Physiology
• Main Authors: CASSANO, Giuseppe, Maffia, M, Ramires, P. A, Vilella, S, Storelli, C.
• Other Authors: Cassano, Giuseppe
• Format: Article in Journal/Newspaper
• Language: English
• Published: 1990
• Subjects: amino acid transport; animal cell; article; brush border vesicle; fish; intestine; nonhuman; priority journal; sodium transport; Anguilla anguilla
• Online Access: http://hdl.handle.net/11586/140353; https://doi.org/10.1016/0300-9629(90)90035-Q

1. 1. Kinetics of Na-neutral amino acid cotransport by brush-border membrane vesicles from the eel (Anguilla anguilla) intestine was studied. 2. 2. The substrate-dependent Na-influx was estimated by monitoring the decay of a preset inside negative membrane potential with a voltage-sensitive fluorescent dye. 3. 3. N-Methylglycine, N-methylalanine and α-(methylamino)-isobutyric acid are transported by the Na-dependent carrier responsible for proline translocation. This carrier is distinct from the one responsible for glycine, alanine and α-aminoisobutyric acid translocation.