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Titolo:
Irreversible site-directed labeling of the 4-aminobutyrate binding site bytritiated mefa-sulfonate benzene diazonium - Contribution of a nucleophilic amino acid residue of the alpha 1 subunit
Autore:
Jacques, P; Perret, F; Bouchet, MJ; Foucaud, B; Goeldner, M; Benke, D;
Indirizzi:
Univ Strasbourg 1, Fac Pharm, Chim Bioorgan Lab, Strasbourg, France Univ Strasbourg 1 Strasbourg France im Bioorgan Lab, Strasbourg, France ETH, Inst Pharmacol, Zurich, Switzerland ETH Zurich SwitzerlandETH, Inst Pharmacol, Zurich, Switzerland Univ Zurich, CH-8006 Zurich, Switzerland Univ Zurich Zurich Switzerland CH-8006 rich, CH-8006 Zurich, Switzerland
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 1, volume: 265, anno: 1999,
pagine: 189 - 194
SICI:
0014-2956(199910)265:1<189:ISLOT4>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
GABA(A) RECEPTOR SUBTYPES; BENZODIAZEPINE RECEPTOR; AFFINITY LABEL; BETA-SUBUNIT; PHARMACOLOGY; PROTEINS; CHANNELS; ACETYLCHOLINESTERASE; IDENTIFICATION; QUANTITATION;
Keywords:
affinity labeling; membrane protein purification; receptor structure;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Goeldner, M Univ Strasbourg 1, Fac Pharm, Chim Bioorgan Lab, CNRS,UMR 7514, BP 24, F-67401 Illkirch, France Univ Strasbourg 1 BP 24 Illkirch France F-67401 kirch, France
Citazione:
P. Jacques et al., "Irreversible site-directed labeling of the 4-aminobutyrate binding site bytritiated mefa-sulfonate benzene diazonium - Contribution of a nucleophilic amino acid residue of the alpha 1 subunit", EUR J BIOCH, 265(1), 1999, pp. 189-194

Abstract

Tritiated meta-sulfonate benzene diazonium ([H-3]MSBD), a molecule structurally related to 4-aminobutyrate (GABA), which presents a reactivity towardnucleophilic amino acid residues, was synthesized to investigate the GABA binding site on the GABA(A) receptor. Irreversible labeling reactions using[H-3]MSBD were performed on purified GABA(A) receptors isolated from cow brain membranes and labeled receptors were analyzed by SDS/PAGE. [H-3]MSBD was found to be specifically incorporated into proteins in the 45-60 kDa molecular mass range which were identified as al subunits and beta 2/beta 3 subunits by immunoprecipitation with subunit-specific antibodies. The specific immunoprecipitation of alpha and beta subunits confirms that binding of [H-3]MSBD occurs at the boundary of these subunits. These labeling results confirm the involvement of nucleophilic residues from the beta subunit but reveal also the contribution of yet unidentified nucleophilic residues on the cu subunit for the GABA binding site.

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Documento generato il 08/04/20 alle ore 08:58:13