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PMID:18189341
| Citation |
Meyer, EH, Taylor, NL and Millar, AH (2008) Resolving and identifying protein components of plant mitochondrial respiratory complexes using three dimensions of gel electrophoresis. J. Proteome Res. 7:786-94 |
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| Abstract |
Analyzing highly hydrophobic proteins is a challenge for identification protocols based on gel separation and mass spectrometry. We combined Blue Native and 2D tricine gel electrophoresis to allow separation and identification of respiratory complex subunits from Arabidopsis mitochondria. We identified many of the highly hydrophobic mitochondrion-encoded subunits (GRAVY scores between +0.6 to +1.4) and also found a number of nucleus-encoded proteins associated with complex I for the first time in plants. |
| Links |
PubMed Online version:10.1021/pr700595p |
| Keywords |
Amino Acid Sequence; Animals; Arabidopsis/metabolism; Arabidopsis Proteins/chemistry; Arabidopsis Proteins/isolation & purification; Arabidopsis Proteins/metabolism; Cattle; Cell Respiration/physiology; Electron Transport Complex I/chemistry; Electron Transport Complex I/isolation & purification; Electron Transport Complex III/chemistry; Electron Transport Complex III/isolation & purification; Electrophoresis, Gel, Two-Dimensional; Humans; Mitochondria/chemistry; Mitochondria/metabolism; Mitochondrial Proteins/chemistry; Mitochondrial Proteins/isolation & purification; Mitochondrial Proteins/metabolism; Molecular Sequence Data; Spectrometry, Mass, Electrospray Ionization |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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