Sulfhydryl reactivity of human erythrocyte superoxide dismutase. On the origin of the unusual spectral properties of the protein when prepared by a procedure utilizing chloroform and ethanol for the precipitation of hemoglobin.

@article{Briggs1978SulfhydrylRO,
  title={Sulfhydryl reactivity of human erythrocyte superoxide dismutase. On the origin of the unusual spectral properties of the protein when prepared by a procedure utilizing chloroform and ethanol for the precipitation of hemoglobin.},
  author={Robert G. Briggs and James A. Fee},
  journal={Biochimica et biophysica acta},
  year={1978},
  volume={537 1},
  pages={100-9}
}
1. During purification of human superoxide dismutase by the McCord-Fridovich procedure (McCord, J.M. and Fridovich, I. (1969) J. Biol. Chem. 244, 6049--6055) the "extra" sulfhydryl groups react with a variety of sulfur containing compounds including zero-valent sulfur to yield several dismutase fractions containing excess sulfur atoms and having a unique absorption band in the region of 325 nm. This is shown to be artefact of the purification procedure. 2. Cysteine trisulfide and glutathione… CONTINUE READING

References

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KgL Norske Videnskab

E. Bernt, H. U. Bergmeyer
Biochem. Biophys. Res. Comm • 1945

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