Ligand-dependent Bohr effect of Chrionomus hemoglobins.

  title={Ligand-dependent Bohr effect of Chrionomus hemoglobins.},
  author={Gerd J. Steffens and Gerhard Buse and Axel Wollmer},
  journal={European journal of biochemistry},
  volume={72 1},
The O2 and CO Bohr effects of monomeric and dimeric hemoglobins of the insect Chironomus thummi thummi were determined as proton releases upon ligation. For the O2 Bohr effect of the monomeric hemoglobin III a maximum value of 0.20 H+/heme was obtained at pH 7.5. Upon ligation with CO, however, only 0.04 H+/heme were released at the same pH. In agreement with this finding isoelectric focusing experiments revealed different isoelectric points for O2-liganded and CO-liganded states of hemoglobin… CONTINUE READING

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