Abstract
Publisher Summary This chapter discusses the different methods on the affinity purification of cytochrome-c reductase from potato, the electrophoretic characterization of the isolated enzyme complex, the separation of single subunits from the complex, the analysis of enzymatic activities, the determination of the primary structure of the subunits, and the investigation of the biogenesis of the complex. Many of the procedures presented were originally developed for the investigation of the respiratory chain from mammals and fungi and have been adapted or modified for studying the enzyme complex from higher plants. The biochemical, physiological, and molecular genetic methods presented in this chapter provide unequivocal proof for the complete integration of the general mitochondrial processing peptidase into the cytochrome-c reductase complex from potato. The bifunctional complex has, therefore, been termed cytochrome-c reductase/processing peptidase complex. Cytochrome-c affinity chromatography is a powerful tool for the isolation of the complex from potato. It also proved to be a gentle, simple, and effective method for the purification of this complex from other plant sources.
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