THE HYBRIDIZATION OF DONKEY AND MOUSE HEMOGLOBINS

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Abstract
Two hybrid components have been prepared from mixtures of donkey and mouse hemoglobins: [alpha]2 D [beta]2 M and [alpha]2 M [beta]2 D. The oxygenation properties of these hemoglobins have been determined and compared with donkey and mouse hemoglobins. [alpha]2 D [beta]2 M has an oxygen affinity and Bohr effect (proton discharge during oxygenation) characteristic of mouse hemoglobin. In contrast, [alpha]2 M [beta]2 D has the oxygenation properties of donkey hemoglobin. We conclude that the [beta]-chain controls the physiological function of the hemoglobin molecule and has played a special role in evolution not shared by the [alpha]-chain.