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dc.contributor.author
Antollini, Silvia Susana
dc.contributor.author
Barrantes, Francisco Jose
dc.date.available
2018-07-25T15:49:11Z
dc.date.issued
2002-01-11
dc.identifier.citation
Antollini, Silvia Susana; Barrantes, Francisco Jose; Unique effects of different fatty acid species on the physical properties of the Torpedo acetylcholine receptor membrane; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 277; 2; 11-1-2002; 1249-1254
dc.identifier.issn
0021-9258
dc.identifier.uri
http://hdl.handle.net/11336/53079
dc.description.abstract
To study the effects produced by free fatty acids (FFA) on the biophysical properties of Torpedo marmorata nicotinic acetylcholine receptor-rich native membranes and to investigate the topology of their binding site(s), fluorescence measurements were carried out using the fluorescent probe Laurdan (6-dodecanoyl-2-(dimethyl-amino) naphthalene) and ADIFAB, an Acrylodan-derivatized intestinal fatty acid-binding protein. The generalized polarization (GP) of the former probe was used to learn about the physical state of the membrane upon FFA binding. Saturated FFA induced a slight increase in GP, whereas cis-unsaturated fatty acids decreased GP. Double bond isomerism could also be distinguished; oleic acid (18:1cis) induced a net disordering effect, whereas elaidic acid (18:1trans) produced no changes in GP. The changes in the efficiency of the Förster energy transfer from the protein to Laurdan brought about by addition of FFA, together with the distances involved in this process, indicate that all FFA studied share a common site at the lipid-protein interface. However, despite being located at the same site, each class of FFA differs in its effect on the physical properties of the membrane. These data lead us to suggest that it is the direct action of FFA at the lipid-protein interface, displacing essential lipids from their sites rather than changes in bulk properties such as membrane fluidity that accounts for the effect of FFA on the acetylcholine receptor membrane.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Society for Biochemistry and Molecular Biology
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by/2.5/ar/
dc.subject
Ácido Graso
dc.subject
Achr
dc.subject.classification
Otras Ciencias Biológicas
dc.subject.classification
Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Unique effects of different fatty acid species on the physical properties of the Torpedo acetylcholine receptor membrane
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-07-11T14:11:03Z
dc.journal.volume
277
dc.journal.number
2
dc.journal.pagination
1249-1254
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Bethesda
dc.conicet.avisoEditorial
This research was originally published in the Journal of Biological Chemistry. Silvia S. Antollini and Francisco J. Barrantes. Unique Effects of Different Fatty Acid Species on the Physical Properties of the Torpedo Acetylcholine Receptor Membrane. Journal of Biological Chemistry. 2002; 277 (22):1249-1254. © the American Society for Biochemistry and Molecular Biology or © the Author(s).
dc.description.fil
Fil: Antollini, Silvia Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina. Unesco; Argentina
dc.description.fil
Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina. Unesco; Argentina
dc.journal.title
Journal of Biological Chemistry (online)
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1074/jbc.M106618200
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/277/2/1249.full
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