Trematode hemoglobins show exceptionally high oxygen affinity.

@article{Kiger1998TrematodeHS,
  title={Trematode hemoglobins show exceptionally high oxygen affinity.},
  author={Laurent Kiger and A. R. Khalim Rashid and Nathalie Griffon and Masudul Haque and L. Moens and Quentin Howieson Gibson and Claude Poyart and Michael C. Marden},
  journal={Biophysical journal},
  year={1998},
  volume={75 2},
  pages={
          990-8
        }
}
Ligand binding studies were made with hemoglobin (Hb) isolated from trematode species Gastrothylax crumenifer (Gc), Paramphistomum epiclitum (Pe), Explanatum explanatum (Ee), parasitic worms of water buffalo Bubalus bubalis, and Isoparorchis hypselobagri (Ih) parasitic in the catfish Wallago attu. The kinetics of oxygen and carbon monoxide binding show very fast association rates. Whereas oxygen can be displaced on a millisecond time scale from human Hb at 25 degrees C, the dissociation of… CONTINUE READING
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