Effect of Cl- and H+ on the oxygen binding properties of glutaraldehyde-polymerized bovine hemoglobin-based blood substitutes.
Bovine hemoglobin was cross-linked with glutaraldehyde, resulting in high oxygen affinity polymeric hemoglobin dispersions of varying molecular weight distributions. High oxygen affinity acellular oxygen carriers were designed in order to exhibit oxygen release profiles closer to that of human red blood cells (RBCs), without exhibiting the inherent increased vasoactivity that occurs with low oxygen affinity acellular oxygen carriers (1, 2). Oxygen dissociation curves were measured for polymerized hemoglobin dispersions at various pH values (7.0, 7.4, and 8.0) and chloride ion concentrations. Unmodified hemoglobin showed an increase in oxygen affinity with increased chloride ion concentration and a decrease in oxygen affinity with increased pH, as was previously demonstrated in the literature (3). For glutaraldehyde-polymerized hemoglobin dispersions, the ability of the oxygen affinity to respond to changes in Bohr H+ and Cl- concentration was weakened. However, at acidic physiological pH (pH = 7), the Bohr effect was still present at high Cl- concentrations. Thus, the Bohr effect maintained some dependency on the Cl- concentration.
Department of Chemical and Biomolecular Engineering, University of Notre Dame, Notre Dame, Indiana 46556, USA.
Julie H
JH
Eike
Andre F
AF
Palmer
D000818:Animals; D001665:Binding Sites; D001802:Blood Substitutes / Q000737:chemistry*; D002417:Cattle; D002713:Chlorine / Q000737:chemistry*; D003432:Cross-Linking Reagents / Q000737:chemistry; D005976:Glutaral / Q000737:chemistry*; D006454:Hemoglobins / Q000737:chemistry*; D006859:Hydrogen / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D010084:Oxidation-Reduction; D010100:Oxygen / Q000737:chemistry*; D011485:Protein Binding
D001802:Blood Substitutes; D003432:Cross-Linking Reagents; D006454:Hemoglobins; D002713:Chlorine; D006859:Hydrogen; D010100:Oxygen; D005976:Glutaral