Purification and characterization of cytochrome c oxidase from the insect trypanosomatid Crithidia fasciculata

D. Speijer, A. O. Muijsers, H. Dekker, A. de Haan, C. K. Breek, S. P. Albracht, R. Benne

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Cytochrome c oxidase was purified from the mitochondrial lysate of the insect trypanosomatid Crithidia fasciculata with the aid of a methyl hydrophobic interaction column in a rapid one-step procedure. The purified complex displayed all characteristics expected from a eukaryotic cytochrome c oxidase: the presence of CuA in electron paramagnetic resonance analysis, a characteristic 605 nm peak in reduced-minus-oxidized optical spectroscopy, and the capacity to efficiently oxidize homologous, but not heterologous, cytochrome c. Two-dimensional PAGE showed that C. fasciculata cytochrome c oxidase consists of at least 10 different subunits. N-terminal sequences were obtained from the six smallest subunits of the complex, one of them showing significant similarity to Neurospora crassa cytochrome c oxidase subunit V. The N-terminus of each of the four largest subunits was found to be blocked
Original languageEnglish
Pages (from-to)47-59
JournalMolecular and biochemical parasitology
Issue number1
Publication statusPublished - 1996

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