Two electrophoretically distinguishable hemoglobins have been identified in the bloods of pure bred Dorset sheep. The oxygen affinity of the whole blood, as judged by the oxygen pressure required to half-saturate its hemoglobin at 380 C. and pH 7-4 has been shown to be correlated with the relative proportions of the two hemoglobins. Blood containing only the hemoglobin which moves the more rapidly in the electrophoretic field has a higher oxygen affinity than the one with the lower mobility. The two hemoglobins appear to differ in the amino acid sequence in the beta chain of the molecule.DIURING a study of the adaptations made by pregnant ewes and their fetuses to the low oxygen pressure of high altitude, oxygen dissociation curves of bloods of a number of sheep of Merino stock were prepared at Morococha, Peru in the autumn of 1958 . The results demonstrated a lack of uniformity in the oxygen affinities of the bloods of the individual ewes, for some were half-saturated at an oxygen tension of 31.5-33 mm. Hg at plasma pH 7.4 and 380 C., whereas to saturate others to the same degree, in the same circumstances, required an oxygen tension of 36-38 mm. A similar study on the bloods of pedigree Dorsets at sea level [Meschia et al., 1961 b] revealed a comparable variation in their oxygen affinities.Differences in the oxygen affinities of the bloods of individuals of the same species, when compared at the same plasma pH, could be the result of: (1) differences in their hemoglobins, (2) differences in the concentrations of other solutes within the red cell (intracellular pH, etc.) or (3) a combination of the two circumstances. These factors by their effects on the oxygen affinity of whole blood can play an important role in the regulation of the circulation and respiration of the individual. Yet there is at present no agreement of the relative importance of these possible sources of variation.In an effort to learn something of the relative importance of the structure