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

doi:https://doi.org/10.1016/0166-6851(96)02648-5

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

Research output: Contribution to journal › Article › Academic › peer-review

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Abstract

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 language	English
Pages (from-to)	47-59
Journal	Molecular and Biochemical Parasitology
Volume	79
Issue number	1
DOIs	https://doi.org/10.1016/0166-6851(96)02648-5
Publication status	Published - 1996

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https://doi.org/10.1016/0166-6851(96)02648-5

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@article{427ebb77759a4661939170721ca4ee67,

title = "Purification and characterization of cytochrome c oxidase from the insect trypanosomatid Crithidia fasciculata",

abstract = "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",

author = "D. Speijer and Muijsers, {A. O.} and H. Dekker and {de Haan}, A. and Breek, {C. K.} and Albracht, {S. P.} and R. Benne",

year = "1996",

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T1 - Purification and characterization of cytochrome c oxidase from the insect trypanosomatid Crithidia fasciculata

AU - Speijer, D.

AU - Muijsers, A. O.

AU - Dekker, H.

AU - de Haan, A.

AU - Breek, C. K.

AU - Albracht, S. P.

AU - Benne, R.

PY - 1996

Y1 - 1996

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AB - 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

U2 - https://doi.org/10.1016/0166-6851(96)02648-5

DO - https://doi.org/10.1016/0166-6851(96)02648-5

M3 - Article

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