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Composition of raft-like cell membrane microdomains resistant to styrene-maleic acid copolymer (SMA) solubilization.
Harant, Karel; Cajka, Tomás; Angelisová, Pavla; Pokorná, Jana; Horejsí, Václav.
Afiliação
  • Harant K; Proteomics Core Facility, Faculty of Science, Charles University, BIOCEV, Prumyslova 595, Vestec CZ-25242, Czechia; Institute for Environmental Studies, Faculty of Science, Charles University, Benatska 2, Prague 2 CZ-128 01, Czechia. Electronic address: karel.harant@natur.cuni.cz.
  • Cajka T; Institute of Physiology of the Czech Academy of Sciences, Vídenská, 1083 142 20 Praha 4, Czechia. Electronic address: Tomas.Cajka@fgu.cas.cz.
  • Angelisová P; Institute of Molecular Genetics of the Czech Academy of Sciences, Vídenská, 1083 142 20 Praha 4, Czechia.
  • Pokorná J; Institute of Molecular Genetics of the Czech Academy of Sciences, Vídenská, 1083 142 20 Praha 4, Czechia.
  • Horejsí V; Institute of Molecular Genetics of the Czech Academy of Sciences, Vídenská, 1083 142 20 Praha 4, Czechia. Electronic address: vaclav.horejsi@img.cas.cz.
Biophys Chem ; 296: 106989, 2023 05.
Article em En | MEDLINE | ID: mdl-36898346
An advantageous alternative to the use of detergents in biochemical studies on membrane proteins are the recently developed styrene-maleic acid (SMA) amphipathic copolymers. In our recent study [1] we demonstrated that using this approach, most T cell membrane proteins were fully solubilized (presumably in small nanodiscs), while two types of raft proteins, GPI-anchored proteins and Src family kinases, were mostly present in much larger (>250 nm) membrane fragments markedly enriched in typical raft lipids, cholesterol and lipids containing saturated fatty acid residues. In the present study we demonstrate that disintegration of membranes of several other cell types by means of SMA copolymer follows a similar pattern and we provide a detailed proteomic and lipidomic characterization of these SMA-resistant membrane fragments (SRMs).
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Texto completo: 1 Bases de dados: MEDLINE Assunto principal: Poliestirenos / Proteômica Idioma: En Revista: Biophys Chem Ano de publicação: 2023 Tipo de documento: Article

Texto completo: 1 Bases de dados: MEDLINE Assunto principal: Poliestirenos / Proteômica Idioma: En Revista: Biophys Chem Ano de publicação: 2023 Tipo de documento: Article