Influence of allosteric effectors and temperature on oxygen binding properties and the Bohr effect of bovine hemoglobin.

The O2 binding properties of bovine Hb were examined. The increase in Cl- and DPG concentration enhanced P50. A reduction in n(max) was observed at high Cl- concentration, while DPG had little effect on n(max).

Contribution of cooperativity and the Bohr effect to efficient oxygen transport by hemoglobins from five mammalian species.

By using published experimental values of the standard oxygen (O2) equilibrium curve and the in vivo arterial and venous O2 pressure (PO2) of fetal and maternal blood in five mammalian species (human, cow, pig, sheep, and horse), we investigated the relationship between the efficiency of O2 delivery and the effectiveness of the Bohr shift, and discussed the significance of cooperativity for mammalian Hb. The O2 delivery of fetal blood was more efficient than that of maternal blood, and the effectiveness of the Bohr shift at both O2 loading and release sites of fetal blood was high. A linear relationship was observed between the efficiency of O2 delivery and the effectiveness of the Bohr shift at O2 loading sites of the five mammalian species.

Significance of affinity and cooperativity in oxygen binding to hemoglobin of horse fetal and maternal blood.

The physiological significance of the position and shape of the oxygen equilibrium curve (OEC) of horse hemoglobin (Hb) is considered from the viewpoint of oxygen (O2) transport efficiency and the effectiveness of the Bohr effect. In horse fetal and maternal bloods, their physiological O2 affinities are nearly optimized with respect to the effectiveness of the Bohr shift occurring at the O2 release site, when it is measured by the change in O2 saturation per unit change in P50. With relatively low cooperativity (n=2.

The cooperativity of human fetal and adult hemoglobins is optimized: a consideration based on the effectiveness of the Bohr shift.

The physiological significance of the cooperativity of human hemoglobin (Hb) is considered from the viewpoint of the effectiveness of the Bohr shift at the sites of O(2) release and uptake across the placental membrane. The effects of the Bohr shift was examined by changing the O(2) saturation of Hb (S(pO2)) per unit change in P(50), -dS(PO2)/d P(50), where P(50) is partial pressure of O(2) at half saturation. The Bohr shift at the sites of O(2) uptake and release was found to be highly effective in both fetal and maternal bloods at physiological degree of cooperativity (Hill's coefficient, n=2.