Abstract
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 language | English |
|---|---|
| Pages (from-to) | 111-115 |
| Number of pages | 5 |
| Journal | Biophysical Chemistry |
| Volume | 38 |
| Issue number | 1-2 |
| DOIs | |
| State | Published - Oct 1990 |
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Keywords
- Halide effect
- Hemoglobin
- Oxygen affinity
- Temperature effect
- Van't Hoff enthalpy
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Effect of temperature on oxygen affinity and anion binding of bovine hemoglobin. / Razynska, Anna; Fronticelli, Clara; Di Cera, Enrico; Gryczynski, Zygmunt; Bucci, Enrico.
In: Biophysical Chemistry, Vol. 38, No. 1-2, 10.1990, p. 111-115.Research output: Contribution to journal › Article
TY - JOUR
T1 - Effect of temperature on oxygen affinity and anion binding of bovine hemoglobin
AU - Razynska, Anna
AU - Fronticelli, Clara
AU - Di Cera, Enrico
AU - Gryczynski, Zygmunt
AU - Bucci, Enrico
PY - 1990/10
Y1 - 1990/10
N2 - 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.
AB - 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.
KW - Halide effect
KW - Hemoglobin
KW - Oxygen affinity
KW - Temperature effect
KW - Van't Hoff enthalpy
UR - http://www.scopus.com/inward/record.url?scp=0025083377&partnerID=8YFLogxK
U2 - 10.1016/0301-4622(90)80045-9
DO - 10.1016/0301-4622(90)80045-9
M3 - Article
C2 - 2085646
AN - SCOPUS:0025083377
VL - 38
SP - 111
EP - 115
JO - Biophysical Chemistry
JF - Biophysical Chemistry
SN - 0301-4622
IS - 1-2
ER -