Proteomic Analysis of Succinate Dehydrogenase and Ubiquinol-cytochrome C Reductase (Complex Ii and Iii) Isolated by Immunoprecipitation from Bovine and Mouse Heart Mitochondria.
From: Buck Institute for Age Research, Novato, CA 94945, USA.
Biochimica et biophysica acta
- Publish Date: Feb 2006
- ISSN: 0006-3002
- Volume: 1762
- Issue: 2
- Pages: 213-22
- Medium: Print
- Language: English
- Citation (JAMA): Schilling Birgit, Murray James, Yoo Chris B, et al. Proteomic Analysis of Succinate Dehydrogenase and Ubiquinol-cytochrome C Reductase (Complex Ii and Iii) Isolated by Immunoprecipitation from Bovine and Mouse Heart Mitochondria.. Biochim. Biophys. Acta Feb 2006;1762:213-22
Abstract
The oxidative phosphorylation system (OXPHOS) consists of five multi-enzyme complexes, Complexes I-V, and is a key component of mitochondrial function relating to energy production, oxidative stress, cell signaling and apoptosis. Defects or a reduction in activity in various components that make up the OXPHOS enzymes can cause serious diseases, including neurodegenerative disease and various metabolic disorders. Our goal is to develop techniques that are capable of rapid and in-depth analysis of all five OXPHOS complexes. Here, we describe a mild, micro-scale immunoisolation and mass spectrometric/proteomic method for the characterization of Complex II (succinate dehydrogenase) and Complex III (ubiquinol-cytochrome c reductase) from bovine and rodent heart mitochondria. Extensive protein sequence coverage was obtained after immunocapture, 1D SDS PAGE separation and mass spectrometric analysis for a majority of the 4 and 11 subunits, respectively, that make up Complexes II and III. The identification of several posttranslational modifications, including the covalent FAD modification of flavoprotein subunit 1 from Complex II, was possible due to high mass spectrometric sequence coverage.
Mesh Headings (Keywords): Amino Acid Sequence, Animals, Cattle, Electron Transport Complex III, Immunoprecipitation, Mass Spectrometry, Mice, Mitochondria, Heart, Molecular Sequence Data, Protein Processing, Post-Translational, Protein Subunits, Proteomics, Succinate Dehydrogenase
Check for Full Text / PubMed Unique Identifier (PMID): 16120479
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.