Purification and characterization of 33 kilodalton protein of spinach chloroplasts.

@article{Kuwabara1979PurificationAC,
  title={Purification and characterization of 33 kilodalton protein of spinach chloroplasts.},
  author={Takaaki Kuwabara and Norio Murata},
  journal={Biochimica et biophysica acta},
  year={1979},
  volume={581 2},
  pages={
          228-36
        }
}
  • Takaaki Kuwabara, Norio Murata
  • Published in Biochimica et biophysica acta 1979
  • Chemistry, Medicine
  • A protein was prepared from spinach chloroplasts in a highly purified form. The isoelectric point of the protein was 5.2. The apparent molecular weight was estimated to be 33 000 by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and urea, and 34 000 by gel filtration column chromatography with Sephadex G-100. The protein was provisionally named '33 kilodalton protein' according to the molecular weight. The absorption spectrum of the protein did not show any… CONTINUE READING

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