Oxygen equilibrium curve shape and allohemoglobin interaction in sheep whole blood

L. A. Maginniss, A. J. Olszowka and R. B. Reeves Adult sheep (Ovis aries) exhibit hemoglobin heterogeneity controlled by two autosomal alleles with codominant expression (Hb AA, AB, BB). Isoelectric points for Hb A and Hb B were 6.94 and 7.15, respectively; for Hb AB animals, the two allohemoglobins were present in equimolar concentrations (Hb A = 52%, Hb B = 48%). Dynamic O2 equilibrium curves (O2ECs) were generated for sheep whole blood at 39 degrees C using thin-film techniques. Half-saturation PO2 values (P50) at pH 7.50 were 31.3, 35.7, and 40.7 Torr for Hb AA, AB, and BB, respectively. CO2 Bohr coefficients at saturation (S) = 0.5 (delta log P50/delta pH) were similar for all phenotypes, ranging from -0.38 to -0.40. The Bohr slopes were also saturation independent between 0.2 and 0.8 S. Standard O2ECs for each phenotype were accurately fitted to three-constant third-order polynomial expressions. Sheep equilibrium curves were not isomorphic with other mammalian O2ECs (e.g., human and dog); sheep curves exhibited greater sigmoidicity. Furthermore, allohemoglobin interaction was not detected in heterozygous sheep. The blood O2 binding characteristics (P50, curve shape, and delta log PO2/delta pH) for Hb AB sheep and an experimental blood mixture containing equal proportions of Hb AA and Hb BB erythrocytes were equivalent.