Biphasic nature in the autoxidation reaction of human oxyhemoglobin.

@article{Tsuruga1997BiphasicNI,
  title={Biphasic nature in the autoxidation reaction of human oxyhemoglobin.},
  author={Mie Tsuruga and Keiji Shikama},
  journal={Biochimica et biophysica acta},
  year={1997},
  volume={1337 1},
  pages={
          96-104
        }
}
  • Mie Tsuruga, Keiji Shikama
  • Published in Biochimica et biophysica acta 1997
  • Chemistry, Medicine
  • In comparison with myoglobin molecule as a reference, we have studied the autoxidation rate of human oxyhemoglobin (HbO2) as a function of its concentration in 0.1 M buffer at 35 degrees C and in the presence of 1 mM EDTA. At pH 6.5, HbA showed a biphasic autoxidation reaction that can be described completely by a first-order rate equation containing two rate constants-kf, for fast autoxidation of the alpha-chain, and ks, for slow autoxidation of the beta-chain, respectively. When tetrameric… CONTINUE READING

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    Comparative analysis of autoxidation of haemoglobin.

    • Frank B Jensen
    • Biology, Medicine
    • The Journal of experimental biology
    • 2001
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