PuSH - Publication Server of Helmholtz Zentrum München: Native fractionation: isolation of native membrane-bound protein complexes from porcine rod outer segments using isopycnic density gradient centrifugation.

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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)

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Open Access Green as soon as Postprint is submitted to ZB.

Abstract
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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.*

Corresponding Author

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.]

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) CF Metabolomics & Proteomics (CF-MPC)