STUDIES ON THE HEMOGLOBIN-OXYGEN EQUILIBRIUM.
Final quarterly rept. no. 1, 1 Jan 62-31 May 63,
NARA MEDICAL COLL KASHIHARA CITY (JAPAN)
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The relation between the chemical structure a5d physiological function of hemoglobin was investigated with special reference to the role played by the protein moiety in the oxygen equilibrium function. The oxygenation of hemoglobin accompanies a reversible enormous hyperchromicity in the ultraviolet region and a marked increase in the resistance against alkali denaturation, suggesting a reversible conformation change in the protein moiety during the oxygenation. Heterogeneity of adult rat hemoglobin, which probably consists of six subcomponents, was substantiated by alkali denaturation and salting-out techniques. Fetalmaternal differences in molecular structure of hemoglobin were established in rabbits from the measurement of alkali denaturation rate, reactive SH content, and ultraviolet absorption spectrum, although both the hemoglobins exhibit the same homogeneous pattern on starch-gel electrophoresis. In oxygen equilibrium function, the fetal pigment shows a higher oxygen affinity and less Bohr effect than the maternal one, and these differences are ascribed to the differences in their molecular structure. Author