Purification of a hexaheme cytochrome c552 from Escherichia coli K 12 and its properties as a nitrite reductase.

@article{Kajie1986PurificationOA,
  title={Purification of a hexaheme cytochrome c552 from Escherichia coli K 12 and its properties as a nitrite reductase.},
  author={S Kajie and Yasuhiro Anraku},
  journal={European journal of biochemistry},
  year={1986},
  volume={154 2},
  pages={457-63}
}
Anaerobic cytochrome c552 was purified to electrophoretic homogeneity by ion-exchange chromatography and gel filtration from a mutant of Escherichia coli K 12 that synthesizes an increased amount of this pigment. Several molecular and enzymatic properties of the cytochrome were investigated. Its relative molecular mass was determined to be 69 000 by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. It was found to be an acidic protein that existed in the monomeric form in the native… CONTINUE READING

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