dc.creatorCrepaldi Domingues, C
dc.creatorCiana, A
dc.creatorButtafava, A
dc.creatorBalduini, C
dc.creatorde Paula, E
dc.creatorMinetti, G
dc.date2009
dc.dateJAN
dc.date2014-11-19T19:15:04Z
dc.date2015-11-26T18:05:11Z
dc.date2014-11-19T19:15:04Z
dc.date2015-11-26T18:05:11Z
dc.date.accessioned2018-03-29T00:47:29Z
dc.date.available2018-03-29T00:47:29Z
dc.identifierJournal Of Membrane Biology. Springer, v. 227, n. 1, n. 39, n. 48, 2009.
dc.identifier0022-2631
dc.identifierWOS:000262125100004
dc.identifier10.1007/s00232-008-9142-4
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/70987
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/70987
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/70987
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1293070
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionLipid rafts are microdomains enriched in cholesterol and sphingolipids that contain specific membrane proteins. The resistance of domains to extraction by nonionic detergents at 4A degrees C is the commonly used method to characterize these structures that are operationally defined as detergent-resistant membranes (DRMs). Because the selectivity of different detergents in defining membrane rafts has been questioned, we have compared DRMs from human erythrocytes prepared with two detergents: Triton X-100 and C12E8. The DRMs obtained presented a cholesterol/protein mass ratio three times higher than in the whole membrane. Flotillin-2 was revealed in trace amounts in DRMs obtained with C12E8, but it was almost completely confined within the DRM fraction with Triton X-100. Differently, stomatin was found distributed in DRM and non-DRM fractions for both detergents. We have also measured the order parameter (S) of nitroxide spin labels inserted into DRMs by means of electron paramagnetic resonance. The 5- and 16-stearic acid spin label revealed significantly higher S values for DRMs obtained with either Triton X-100 or C12E8 in comparison to intact cells, while the difference in the S values between Triton X-100 and C12E8 DRMs was not statistically significant. Our results suggest that although the acyl chain packing is similar in DRMs prepared with either Triton X-100 or C12E8 detergent, protein content is dissimilar, with flotillin-2 being selectively enriched in Triton X-100 DRMs.
dc.description227
dc.description1
dc.description39
dc.description48
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description"Ministero dell'Universita e della Ricerca," Italy
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFAPESP [03/02394-4]
dc.descriptionCAPES [3597/06-7]
dc.descriptionCNPq [141618/2005-1]
dc.languageen
dc.publisherSpringer
dc.publisherNew York
dc.publisherEUA
dc.relationJournal Of Membrane Biology
dc.relationJ. Membr. Biol.
dc.rightsfechado
dc.rightshttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dc.sourceWeb of Science
dc.subjectDetergent-resistant membrane
dc.subjectLipid raft
dc.subjectMembrane-skeleton
dc.subjectEPR
dc.subjectNitroxide spin label
dc.subjectFlotillin
dc.subjectEpr Spin-label
dc.subjectLipid Rafts
dc.subjectCell-membranes
dc.subjectPlasmodium-falciparum
dc.subjectMalarial Infection
dc.subjectAnchored Proteins
dc.subjectSolubilization
dc.subjectCholesterol
dc.subjectSurface
dc.subjectReggie-1/flotillin-2
dc.titleResistance of Human Erythrocyte Membranes to Triton X-100 and C12E8
dc.typeArtículos de revistas


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