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

¹ Division of Biochemistry, Department of Biology, Massachusetts Institute of Technology, Cambridge, Mass. and The Department of Physiology, Yale University School of Medicine, New Haven, Connecticut
² Division of Biochemistry, Department of Biology, Massachusetts Institute of Technology, Cambridge, Mass. and The Department of Physiology, Yale University School of Medicine, New Haven, Connecticut; Department of Biophysics, Johns Hopkins Medical School, Baltimore, Maryland
³ Division of Biochemistry, Department of Biology, Massachusetts Institute of Technology, Cambridge, Mass. and The Department of Physiology, Yale University School of Medicine, New Haven, Connecticut; Department of Pediatrics, Johns Hopkins Medical School, Baltimore, Maryland
⁴ Division of Biochemistry, Department of Biology, Massachusetts Institute of Technology, Cambridge, Mass. and The Department of Physiology, Yale University School of Medicine, New Haven, Connecticut; Department of Gynecology-Obstetrics, Johns Hopkins Medical School, Baltimore, Maryland

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.

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				S. H. Boyer, P. Hathaway, F. Pascasio, C. Orton, J. Bordley, and M. A. Naughton Hemoglobins in Sheep: Multiple Differences in Amino Acid Sequences of Three Beta-Chains and Possible Origins Science, September 23, 1966; 153(3743): 1539 - 1543. [Abstract] [PDF]