Purification and characterization of small molecular weight myeloperoxidase from human promyelocytic leukemia HL-60 cells.

@article{Yamada1981PurificationAC,
  title={Purification and characterization of small molecular weight myeloperoxidase from human promyelocytic leukemia HL-60 cells.},
  author={Michiyuki Yamada and Masatomo Mori and Takashi Sugimura},
  journal={Biochemistry},
  year={1981},
  volume={20 4},
  pages={
          766-71
        }
}
Human myeloperoxidase was purified to homogeneity from human promyelocytic leukemia HL-60 cells. A small molecular weight myeloperoxidase was found in these cells and was separated from three other forms of myeloperoxidase of large molecular weight by carboxymethyl-Sepharose CL-6B column chromatography and Sephacryl S-200 gel filtration. The S20,w values of the molecular weights of the small and large myeloperoxidases were found to be 5.2 and 8.07 S, respectively, by sucrose density gradient… CONTINUE READING

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Lessons from MPO deficiency about functionally important structural features.

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  • 2004
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