Effect of temperature on oxygen affinity and anion binding of bovine hemoglobin

Anna Razynska, Clara Fronticelli, Enrico Di Cera, Zygmunt Gryczynski, Enrico Bucci

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Measurements of oxygen binding to bovine hemoglobin have been carried out over the temperature range 15-37° C at pH 7.33. The standard enthalpy of oxygenation after correction for the heat of oxygen solution and of the Bohr protons is found to be -7.1 or -7.2 kcal/mol in the presence of 0.1 M chloride or bromide, respectively. This value is well below the -14.4 kcal/mol determined for human hemolglobin under identical experimental conditions. As reported by Fronticelli et al. (C. Fronticelli, E. Bucci and A. Razynska, J. Mol. Biol. 202 (1988) 343), the preferential binding of anions by bovine hemoglobin recognizes the various halides. Measurements at various temperatures reveal that this is true only above 25° C. The halide recognition and the less exothermic enthalpy of oxygenation of bovine hemoglobin are probable due to oxygen-linked hydrophobic effects that are larger in bovine than in human hemoglobin.

Original languageEnglish
Pages (from-to)111-115
Number of pages5
JournalBiophysical Chemistry
Issue number1-2
StatePublished - Oct 1990


  • Halide effect
  • Hemoglobin
  • Oxygen affinity
  • Temperature effect
  • Van't Hoff enthalpy


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