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Open Access Green as soon as Postprint is submitted to ZB.
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)
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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Publication type
Article: Journal article
Document type
Scientific Article
Editors
Thompson, J.D.* ; Ueffing, M. ; Schaeffer-Reiss, C.*
Keywords
Density Gradient Centrifugation ; Membrane Proteins ; Nonionic Detergent
ISSN (print) / ISBN
1064-3745
e-ISSN
1940-6029
Conference Title
Functional Proteomics: Methods and Protocols
Journal
Methods in Molecular Biology
Quellenangaben
Volume: 484,
Pages: 161-175
Publisher
Springer
Publishing Place
Berlin [u.a.]
Reviewing status
Peer reviewed
Institute(s)
CF Metabolomics & Proteomics (CF-MPC)