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Titolo:
MULTIPLE COMPONENTS OF ARGININE AND PHENYLALANINE TRANSPORT INDUCED IN NEUTRAL AND BASIC-AMINO-ACID TRANSPORTER CRNA-INJECTED XENOPUS OOCYTES
Autore:
PETER GJ; DAVIDSON IG; AHMED A; MCILROY L; FORRESTER AR; TAYLOR PM;
Indirizzi:
UNIV DUNDEE,DEPT ANAT & PHYSIOL DUNDEE DD1 4HN SCOTLAND UNIV DUNDEE,DEPT ANAT & PHYSIOL DUNDEE DD1 4HN SCOTLAND UNIV ABERDEEN,DEPT CHEM ABERDEEN AB9 2UE SCOTLAND
Titolo Testata:
Biochemical journal
, volume: 318, anno: 1996,
parte:, 3
pagine: 915 - 922
SICI:
0264-6021(1996)318:<915:MCOAAP>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-ERYTHROCYTES; HORSE ERYTHROCYTES; RAT-KIDNEY; EXPRESSION CLONING; LAEVIS OOCYTES; SYSTEM Y(+)L; HEAVY-CHAIN; RBAT; CYSTINURIA; INHIBITION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
G.J. Peter et al., "MULTIPLE COMPONENTS OF ARGININE AND PHENYLALANINE TRANSPORT INDUCED IN NEUTRAL AND BASIC-AMINO-ACID TRANSPORTER CRNA-INJECTED XENOPUS OOCYTES", Biochemical journal, 318, 1996, pp. 915-922

Abstract

The induced uptakes of L-[H-3]phenylalanine and L-[H-3]arginine in oocytes injected with clonal NEAT (neutral and basic amino acid transporter) cRNA show differential inactivation by pretreatment with N-ethylmaleimide (NEM), revealing at least two distinct transport processes. NEM-resistant arginine transport is inhibited by leucine and phenylalanine but not by alanine or valine; mutual competitive inhibition of NEM-resistant uptake of arginine and phenylalanine indicates that the twoamino acids share a single transporter. NEM-senstive arginine transport is inhibited by leucine, phenylalanine, alanine and valine. At least two NEM-sensitive transporters may be expressed because we have beenunable to confirm mutual competitive inhibition between arginine and phenylalanine transport. The NEM-resistant transport mechanism appearsto involve distinct but overlapping binding sites for cationic and zwitterionic substrates. NEAT is known to form oligomeric protein complexes in cell membranes, and its functional roles when expressed in Xenopus oocytes may include interaction with oocyte proteins, leading to increased native amino acid transport activities; these resemble NEAT-expressed activities in terms of NEM-sensitivity and apparent substraterange (including an unusual inhibition by beta-phenylalanine).

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/01/21 alle ore 06:50:15