Myoglobin oxygen dissociation by multiwavelength spectroscopy.

@article{Schenkman1997MyoglobinOD,
  title={Myoglobin oxygen dissociation by multiwavelength spectroscopy.},
  author={Kenneth A Schenkman and David R. Marble and David H. Burns and Eric O. Feigl},
  journal={Journal of applied physiology},
  year={1997},
  volume={82 1},
  pages={
          86-92
        }
}
Multiwavelength optical spectroscopy was used to determine the oxygen-binding characteristics for equine myoglobin. Oxygen-binding relationships as a function of oxygen tension were determined for temperatures of 10, 25, 35, 37, and 40 degrees C, at pH 7.0. In addition, dissociation curves were determined at 37 degrees C for pH 6.5, 7.0, and 7.5. Equilibration was achieved with a myoglobin solution, at the desired temperature and pH, and 16 oxygen-nitrogen gas mixtures of known oxygen fraction… 

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