Myeloperoxidase is synthesized as larger phosphorylated precursor.

@article{Hasilik1984MyeloperoxidaseIS,
  title={Myeloperoxidase is synthesized as larger phosphorylated precursor.},
  author={Andrej Hasilik and Regina Pohlmann and Ragnar L. Olsen and Kurt von Figura},
  journal={The EMBO journal},
  year={1984},
  volume={3 11},
  pages={2671-6}
}
Synthesis and processing of myeloperoxidase were examined in metabolically labeled cells of the human promyelocyte line HL-60 and in an in vitro rabbit reticulocyte lysate system directed with HL-60 mRNA. Radioactivity labeled products were isolated by immunoprecipitation and analyzed by gel electrophoresis and fluorography. In vivo, myeloperoxidase was labeled initially as a 85-K glycosylated polypeptide (75 K after treatment with endo-beta-N-acetylglucosaminidase H). This polypeptide was soon… CONTINUE READING

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