Degradation of heme by a soluble peptide of heme oxygenase obtained from rat liver microsomes by mild trypsinization.

@article{Yoshida1991DegradationOH,
  title={Degradation of heme by a soluble peptide of heme oxygenase obtained from rat liver microsomes by mild trypsinization.},
  author={Tetsuya Yoshida and Kazuhiko Ishikawa and Michihiko Sato},
  journal={European journal of biochemistry},
  year={1991},
  volume={199 3},
  pages={729-33}
}
A tryptic peptide of heme oxygenase obtained after solubilization of rat liver microsomes by mild trypsin treatment was purified. The purified peptide gave only a single protein band with a molecular mass of 28 kDa on SDS/PAGE. The tryptic peptide, like the native heme oxygenase, readily bound with substrate heme forming a hemeprotein transiently. The absorption spectra of the ferric, ferrous, ferrous-CO and ferrous-O2 forms of the resulting complex resembled those of the corresponding forms of… CONTINUE READING

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