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Titolo:
LOCALIZATION OF HISTIDINE-RESIDUES RELEVANT FOR THE BINDING OF ALPHA-BUNGAROTOXIN TO THE ACETYLCHOLINE-RECEPTOR ALPHA-SUBUNIT IN V8-PROTEOLYTIC FRAGMENTS
Autore:
LACORAZZA HD; LOPEZ RA; VENERA GD; BONINO MBD;
Indirizzi:
UNIV BUENOS AIRES,FAC FARM & BIOQUIM,INST QUIM & FISICOQUIM BIOL,CONICET,JUNIN 956 RA-1113 BUENOS AIRES DF ARGENTINA UNIV BUENOS AIRES,FAC FARM & BIOQUIM,INST QUIM & FISICOQUIM BIOL,CONICET RA-1113 BUENOS AIRES DF ARGENTINA
Titolo Testata:
Neurochemistry international
fascicolo: 5-6, volume: 28, anno: 1996,
pagine: 557 - 567
SICI:
0197-0186(1996)28:5-6<557:LOHRFT>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
SODIUM DODECYL-SULFATE; TORPEDO-CALIFORNICA; CDNA SEQUENCE; CALF-MUSCLE; BETA-SUBUNIT; AMINO-ACIDS; SYNTHETIC PEPTIDES; MOLECULAR-WEIGHT; SITE; PRECURSOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
54
Recensione:
Indirizzi per estratti:
Citazione:
H.D. Lacorazza et al., "LOCALIZATION OF HISTIDINE-RESIDUES RELEVANT FOR THE BINDING OF ALPHA-BUNGAROTOXIN TO THE ACETYLCHOLINE-RECEPTOR ALPHA-SUBUNIT IN V8-PROTEOLYTIC FRAGMENTS", Neurochemistry international, 28(5-6), 1996, pp. 557-567

Abstract

Histidine residues have been shown to be critical for alpha-BgTx binding to the acetylcholine receptor (Lacorazza et al., 1992; Bouzat et al., 1993; Lacorazza et al., 1995). Receptor subunits from Discopyge tschudii were modified with diethylpyrocarbonate (DEP). DEP treatment produces a concentration-dependent decrease of [I-125]alpha-BgTx bindingto the alpha subunit. The neurotoxin binding capacity was fully restored by adding the nucleophile hydroxylamine. By proteolytic mapping ofthe alpha-subunit with V8-protease, we determined that the binding capacity to the fragment alpha V8-19 decreased 80% by DEP treatment. In addition, the [I-125]alpha-BgTx binding to the same fragment decreasedby 70% when the subunits were reduced and affinity-alkylated. We report the N-terminal sequence of both subunits and V8-fragments (alpha V8-10, alpha V8-13, and alpha V8-18), which constitute a first contribution to the knowledge of the primary structure of the Discopyge tschudii receptor. We propose that the fragment alpha V8-19 contains one or more of the histidine residues involved in the alpha-BgTx binding and probably-includes the Cys alpha 192-193 disulfide bond. Only two histidine residues are present in the extracellular sequence of Torpedo californica for such fragments: His alpha 186 and alpha 204. Copyright (C)1996 Elsevier Science Ltd.

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Documento generato il 03/07/20 alle ore 22:54:28