HEMOGLOBIN CHARACTERISTICS AND THE OXYGEN AFFINITY OF THE BLOODS OF DORSET SHEEP

Abstract

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 38° C. and pH 7·4 has been shown to be correlated with the relative proportions of the two homoglobins. 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. © 1963 The Physiological Society