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- W2086019738 abstract "Abstract Cytochrome c oxidase (COX) was isolated for the first time from corn root mitochondrial extracts by high-performance hydrophobic interaction chromatography with a 50 mM phosphate buffer (pH 7.2), containing 0.01% Tween 20. A 91% recovery of the total enzyme activity was achieved, along with a twelve-fold increase in specific activity. COX activity recovered from the column decreased rapidly with the age of samples. However, most activity was restored on the addition of phospholipid or non-ionic detergent. The crude oxidase was also fractionated with saturated ammonium sulfate in the presence of various detergents. Ionic and non-ionic detergents had variable effects on the release of the enzyme from corn root membrane as well as on its fractionation with ammonium sulfate." @default.
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- W2086019738 date "1988-07-01" @default.
- W2086019738 modified "2023-09-27" @default.
- W2086019738 title "Purification of cytochrome c oxidase from corn root mitochondria by hydrophobic interaction chromatography" @default.
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- W2086019738 doi "https://doi.org/10.1016/s0021-9673(01)94025-7" @default.
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