CINECA IRIS Institutional Research Information System
IRIS è la soluzione IT che facilita la raccolta e la gestione dei dati relativi alle attività e ai prodotti della ricerca. Fornisce a ricercatori, amministratori e valutatori gli strumenti per monitorare i risultati della ricerca, aumentarne la visibilità e allocare in modo efficace le risorse disponibili.
EnglishBrush-border membrane (BBM) vesicles were prepared from the intestine of yellow eels (Anguilla anguilla) by selective precipitation of all other cellular components. The activity of a Na-substrate cotransporter was evaluated by measuring the rate of decay of an inside negative membrane potential with a voltage-sensitive fluorescent dye; the rate of fluorescence quenching decay in the presence of Na was subtracted from the rate of decay in the presence of both cosubstrates. The kinetics of Na-dependent amino acid transport systems were then determined for the neutral amino acids and their N-methylated analogues. It was concluded that N-methylglycine, N-methylalanine and α-(methylamino)-isobutyric acid are transported by the Na-dependent carrier responsible for proline translocation, which is distinct from the one responsible for glycine, alanine and α-aminoisobutyric acid translocations.
| Titolo: | Do neutral amino acids and their N-methylated analogues share the same Na-dependent carrier in brush-border membrane from the eel intestine? |
| Autori: | |
| Data di pubblicazione: | 1990 |
| Rivista: | |
| Abstract: | Brush-border membrane (BBM) vesicles were prepared from the intestine of yellow eels (Anguilla anguilla) by selective precipitation of all other cellular components. The activity of a Na-substrate cotransporter was evaluated by measuring the rate of decay of an inside negative membrane potential with a voltage-sensitive fluorescent dye; the rate of fluorescence quenching decay in the presence of Na was subtracted from the rate of decay in the presence of both cosubstrates. The kinetics of Na-dependent amino acid transport systems were then determined for the neutral amino acids and their N-methylated analogues. It was concluded that N-methylglycine, N-methylalanine and α-(methylamino)-isobutyric acid are transported by the Na-dependent carrier responsible for proline translocation, which is distinct from the one responsible for glycine, alanine and α-aminoisobutyric acid translocations. |
| Handle: | http://hdl.handle.net/11587/105211 |
| Appare nelle tipologie: | Articolo pubblicato su Rivista |
File in questo prodotto:
http://hdl.handle.net/11587/105211
Copyright © 2020