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Lange, M.S.* ; Müller, B.* ; Ueffing, M.

Native fractionation: isolation of native membrane-bound protein complexes from porcine rod outer segments using isopycnic density gradient centrifugation.

Methods Mol. Biol. 484, 161-175 (2008)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
Networks of interacting protein control physiological processes in all living cells. Considerable effort has recently been invested in understanding protein interactions under normal and diseased conditions. One approach to elucidate the composition of protein complexes is native fractionation followed by immunological or MS-based identification of individual compounds. Native fractionation, in contrast to widespread affinity-based purification methods, allows analysis of protein interactions at the endogenous expression level and within a physiological context. In this chapter we describe a protocol for native fractionation of membrane-bound protein complexes from isolated porcine rod outer segments (ROSs). Protein complexes from isolated ROS membranes were solubilized using the nonionic detergent beta-dodecylmaltoside and fractionated by isopycnic sucrose density gradient centrifugation. Immunolabeling of individual sucrose gradient fractions demonstrated colocalization of proteins involved in the phototransduction pathway in photoreceptor outer segments.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Herausgeber Thompson, J.D.* ; Ueffing, M. ; Schaeffer-Reiss, C.*
Korrespondenzautor
Schlagwörter Density Gradient Centrifugation ; Membrane Proteins ; Nonionic Detergent
ISSN (print) / ISBN 1064-3745
e-ISSN 1940-6029
Konferenztitel Functional Proteomics: Methods and Protocols
Zeitschrift Methods in Molecular Biology
Quellenangaben Band: 484, Heft: , Seiten: 161-175 Artikelnummer: , Supplement: ,
Verlag Springer
Verlagsort Berlin [u.a.]
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) CF Metabolomics & Proteomics (CF-MPC)