Temperature independence of the alkaline Bohr effect in pig red cells and pig haemoglobin solutions.
The influence of temperature on the oxygen affinity and the alkaline Bohr effect of pig red cells and pig hemoglobin solutions has been compared to that of human adult red cells and human adult hemoglobin. Pig red cells and pig Hb evidence a lower affinity for oxygen in various conditions of pH, temperature and salt concentration, in the presence as well as in the absence of organic phosphates. It has been observed that the alkaline Bohr effect of pig Hb was reduced by 20-25% compared to Hb A0 and independent of changes in temperature, contrary to human Hb A0. Titrations of pig Hb with C1- indicate a lower heterotropic effect of this anion at low concentration of the salt. It is concluded that this may be the origin of the temperature independence of the alkaline Bohr effect in pig Hb. Conversely, the temperature dependence of the alkaline Bohr effect of Hb A0 should be related to the oxygen-linked binding of C1- at the alpha 1-alpha 2 interface.
D000328:Adult; D000818:Animals; D002712:Chlorides / Q000097:blood; D004163:Diphosphoglyceric Acids / Q000097:blood; D004912:Erythrocytes / Q000378:metabolism*; D006441:Hemoglobin A; D006801:Humans; D006863:Hydrogen-Ion Concentration; D010100:Oxygen / Q000097:blood*; D010108:Oxyhemoglobins / Q000378:metabolism*; D013552:Swine; D013696:Temperature; D013816:Thermodynamics
D002712:Chlorides; D004163:Diphosphoglyceric Acids; D010108:Oxyhemoglobins; C028881:hemoglobin A(0); D006441:Hemoglobin A; D010100:Oxygen