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Titolo:
MOLECULAR-SIZE OF RECOMBINANT ALPHA(1)BETA(1) AND ALPHA(1)BETA(1)GAMMA(2) GABA(A) RECEPTORS EXPRESSED IN SF9 CELLS
Autore:
KNIGHT AR; HARTNETT C; MARKS C; BROWN M; GALLAGER D; TALLMAN J; RAMABHADRAN TV;
Indirizzi:
CEREBRUS LTD,OAKDENE COURT,613 READING RD WOKINGHAM RG41 5UA ENGLAND NEUROGEN CORP BRANFORD CT 06405
Titolo Testata:
Receptors & channels
fascicolo: 1, volume: 6, anno: 1998,
pagine: 1 - 18
SICI:
1060-6823(1998)6:1<1:MORAAA>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
NICOTINIC ACETYLCHOLINE-RECEPTOR; GATED ION-CHANNEL; BENZODIAZEPINE RECEPTOR; QUATERNARY STRUCTURE; CEREBRAL-CORTEX; SUBUNIT; SUBTYPES; STOICHIOMETRY; COMPLEX;
Keywords:
GABA(A); MOLECULAR WEIGHT; RECEPTOR; SF9; SUCROSE DENSITY GRADIENT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
A.R. Knight et al., "MOLECULAR-SIZE OF RECOMBINANT ALPHA(1)BETA(1) AND ALPHA(1)BETA(1)GAMMA(2) GABA(A) RECEPTORS EXPRESSED IN SF9 CELLS", Receptors & channels, 6(1), 1998, pp. 1-18

Abstract

The present study examines the physical properties of recombinant human GABA(A) receptors. The baculovirus/Sf9 cell system was used to express combinations of human GABA(A) receptor subunits: alpha(1) alone, alpha(1) with, beta(1), and alpha(1) with beta(1) and gamma(2). Receptors were solubilized using 1% Triton X-100. In sucrose density gradients containing 150mM NaCl, alpha(1)beta(1) receptor-detergent complexes sedimented more slowly than alpha(1)beta(1)gamma(2) constructs (sedimentation coefficient=7.00+/-0.32 and 8.63+/-0.48S, respectively). Stokes' radii for the two receptor-detergent complexes were determined by gel filtration in Sephacryl S-300. These experiments were performed in the presence of 1M sodium chloride to prevent aggregation. The Stokes'radii for alpha(1)beta(1) and alpha(1)beta(1)gamma(2) receptor-detergent complexes were 9.06 +/- 0.23 and 7,91 i 0,19 nm, respectively. Sedimentation experiments in 1M NaCl revealed similar sedimentation coefficients for alpha(1)beta(1) and alpha(1)beta(1)gamma(2), receptor-detergent complexes (8.79+/-0.59 and 8.46+/-0.72S, respectively). The molecular weight of the alpha(1)beta(1) receptor excluding detergent was estimated to be 281 +/- 19 kDa, that of the alpha(1)beta(1)gamma(2) receptor, 247 +/- 21 kDa. This difference is not statistically significant. Given subunit molecular weights which are close to 50 kDa, this suggested a pentameric structure for the majority of alpha(1)beta(1)gamma(2) receptors, and that alpha(1)beta(1) receptors are not ''assembly intermediates'' with fewer subunits.

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Documento generato il 07/04/20 alle ore 22:53:15