Secondary structure of NADPH: protochlorophyllide oxidoreductase examined by circular dichroism and prediction methods.

@article{Birve1996SecondarySO,
  title={Secondary structure of NADPH: protochlorophyllide oxidoreductase examined by circular dichroism and prediction methods.},
  author={Simon Jonsson Birve and Eva Kihl Selstam and Lennart B-{\AA} Johansson},
  journal={The Biochemical journal},
  year={1996},
  volume={317 ( Pt 2)},
  pages={549-55}
}
To study the secondary structure of the enzyme NADPH: protochlorophyllide oxidoreductase (PCOR), a novel method of enzyme isolation was developed. The detergent isotridecyl poly-(ethylene glycol) ether (Genapol X-080) selectively solubilizes the enzyme from a prolamellar-body fraction isolated from wheat (Triticum aestivum L.). The solubilized fraction was further purified by ion-exchange chromatography. The isolated enzyme was studied by fluorescence spectroscopy at 77 K, and by CD… CONTINUE READING
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Pigment–Protein Complexes in Plastids

  • E. Selstam, A. Widell-Wigge
  • 1993

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