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- W989824421 abstract "Publisher Summary This chapter describes the affinity chromatography purification of cytochrome-c oxidase from bovine heart mitochondria and other sources. In the mitochondrial respiratory chain cytochrome- c oxidase catalyzes the electron transfer from ferrocytochrome c to molecular oxygen. Specific interaction between cytochrome- c oxidase and its electron donor is useful in developing an affinity chromatography purification technique for cytochrome- c oxidase based on cytochrome- c immobilized on a gel matrix. The solubilized proteins are loaded at low salt concentration to a column containing the gel and after washing the column, they are eluted by increasing the ionic strength of the buffer. Various detergents, mainly of the nonionic type, are used in the solubilization step and during the chromatography procedure. If the solubilization step is optimized and the protein of interest can be released from the membrane in a rather selective way, it is possible to purify it to homogeneity in one affinity chromatography step. The chapter describes cytochrome c gels that are used for several purifications." @default.
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- W989824421 date "1986-01-01" @default.
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- W989824421 title "[6] Affinity chromatography purification of cytochrome-c oxidase from bovine heart mitochondria and other sources" @default.
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- W989824421 doi "https://doi.org/10.1016/s0076-6879(86)26008-5" @default.
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