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Rightshifted dextran-hemoglobin as blood substitute
1Department of Biochemistry, University of Toronto, Canada.
Covalent modification of hemoglobin and dextran-hemoglobin by reductive alkylation under aerobic conditions with periodated inositol tetrakisphosphate brought about a rightshifting of their oxygen dissociation curves. The rightshifted dextran-hemoglobin conjugate provided adequate oxygen delivery in macaques exchange-transfused to 90% with respect to their erythrocyte content. The conjugate did not exhibit the nephrotoxicity of free hemoglobin. It was also more resistant to precipitation, and therefore more amenable to viral sterilisation, by ethanol.
Covalent modification of hemoglobin and dextran-hemoglobin by reductive alkylation under aerobic conditions with periodated inositol tetrakisphosphate brought about a rightshifting of their oxygen dissociation curves. The rightshifted dextran-hemoglobin conjugate provided adequate oxygen delivery in macaques exchange-transfused to 90% with respect to their erythrocyte content. The conjugate did not exhibit the nephrotoxicity of free hemoglobin. It was also more resistant to precipitation, and therefore more amenable to viral sterilisation, by ethanol.