Significant efforts have sought to uncover the protein profile ofArabidopsismitochondria to act as a model for the mitochondrial proteome from plants. A combination of techniques have been undertaken to achieve this goal. We outline a basic two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) separation of mitochondrial proteins, in-gel trypsination techniques, complex protein lysate digestions, and the identification of proteins by matrix-assisted laser desorption/ionization (MALDI) and electrospray ionization (ESI) mass spectrometry.
