The oxygen-linked hydrogen ion binding (the Haldane coefficient) of bovine hemoglobin
- 1 November 1976
- journal article
- physiologica
- Published by Springer Nature in Cellular and Molecular Life Sciences
- Vol. 32 (11) , 1437-1439
- https://doi.org/10.1007/bf01937419
Abstract
Summary The Haldane coefficient (the amount of the oxygen-linked hydrogen ion binding of hemoglobin) was determined in bovine erythrolysate (Hb concentration=13.5 mM) by means of the differential titration method with varying PCO2 from 0 to 74 mm Hg and pH from 6.0 to 8.5 at 37°C. The maximum value of the coefficient was found to be 0.49 mM per mM Hb at PCO2=0 and pH 7.20. With increasing of PCO2, the coefficient became smaller in all ranges of pH studied. The coefficient under the conditions of pH 7.20 and PCO2=45 mm Hg that are normally prevailing in the interior of bovine erythrocytes was 0.31.Keywords
This publication has 7 references indexed in Scilit:
- The carbamate equilibrium of bovine hemoglobin at 37 °cRespiration Physiology, 1975
- Interaction of hemoglobin with hydrogen ions, carbon dioxide, and organic phosphates.Physiological Reviews, 1973
- Proton- and Carbamino-linked Oxygen Affinity of Normal Human BloodActa Physiologica Scandinavica, 1972
- Differences in the Interaction of 2,3-Diphosphoglycerate with Certain Mammalian HemoglobinsScience, 1971
- Oxygen-Linked Hydrogen Ion Binding of Human Hemoglobin. Effects of Carbon Dioxide and 2,3-Diphosphoglycerate I. Studies on ErythrolysateScandinavian Journal of Clinical and Laboratory Investigation, 1971
- Study of the Bohr groups of bovine hemoglobinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1969
- MICRODETERMINATION OF OXYHEMOGLOBIN, METHEMOGLOBIN, AND SULFHEMOGLOBIN IN A SINGLE SAMPLE OF BLOODJournal of Biological Chemistry, 1938