Properties of catalase purified from a methanol-grown yeast, Kloeckera sp. 2201.

@article{Mozaffar1986PropertiesOC,
  title={Properties of catalase purified from a methanol-grown yeast, Kloeckera sp. 2201.},
  author={S Mozaffar and Mitsuyoshi Ueda and K Kitatsuji and S. Ohshima A. Shimizu and Masako Osumi and Atsuo Tanaka},
  journal={European journal of biochemistry},
  year={1986},
  volume={155 3},
  pages={527-31}
}
Catalase, a marker enzyme of peroxisomes, was purified to homogeneity from whole cells of Kloeckera sp. 2201 (a strain of Candida boidinii) grown on methanol by means of ammonium sulfate fractionation followed by hydroxyapatite, Sephacryl S-300 and DEAE-Sepharose column chromatographies. Crystallized catalase was brown-coloured and needle-like. The molecular mass of the enzyme was about 240 000 daltons consisting of four identical subunits of 62 000 daltons. The minimum size of catalase… CONTINUE READING

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