dc.creatorRuggiero, AC
dc.creatorMeirelles, NC
dc.date1998
dc.dateJUN
dc.date2014-12-02T16:25:29Z
dc.date2015-11-26T16:18:00Z
dc.date2014-12-02T16:25:29Z
dc.date2015-11-26T16:18:00Z
dc.date.accessioned2018-03-28T23:01:54Z
dc.date.available2018-03-28T23:01:54Z
dc.identifierMolecular Genetics And Metabolism. Academic Press Inc, v. 64, n. 2, n. 148, n. 151, 1998.
dc.identifier1096-7192
dc.identifierWOS:000075520300007
dc.identifier10.1006/mgme.1998.2689
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/79776
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/79776
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/79776
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1267568
dc.descriptionThe chemical modifications induced by trifluoperazine (TFP) in erythrocyte ghosts have been investigated by fluorescence quenching. The apparent distance separating the membrane protein tryptophans and bound 1-aniline-8-naphthalene sulfonate (ANS) molecules decreased after treating erythrocyte membranes with TFP. This effect was accompanied by a significant decrease in the maximum efficiency of energy transfer. We conclude that TFP-induced alterations in the structure of membrane proteins lead to a rearrangement of the surrounding lipids, and consequently to local conformational changes in membrane organization. (C) 1998 Academic Press.
dc.description64
dc.description2
dc.description148
dc.description151
dc.languageen
dc.publisherAcademic Press Inc
dc.publisherSan Diego
dc.publisherEUA
dc.relationMolecular Genetics And Metabolism
dc.relationMol. Genet. Metab.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjecttrifluoperazine
dc.subjecterythrocyte membrane
dc.subjectfluorescence
dc.subjectChlorpromazine
dc.subjectPhenothiazines
dc.titleEffects of trifluoperazine on the conformation and dynamics of membrane proteins in human erythrocytes
dc.typeArtículos de revistas


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