STUDIES ON THE HEMOGLOBIN-OXYGEN EQUILIBRIUM.

Interrelationship between structure and function in hemoglobin was investigated with special reference to the role played by the protein moiety in the oxygenation function. An abnormal hemoglobin showed enormous functional abnormalities 1 a marked reduction in the oxygen affinity, 2 complete absence of Bohr effect and 3 almost complete lacking of heme-heme interaction. By analogy of Hb M sub osaka to Hb H b sub 4 in their structure and function, it was argued that normal function of hemoglobins, as expressed by strong heme-heme interaction, moderate oxygen affinity and normal Bohr effect, requires the presence of and an interaction between the two kinds of polypeptide subunit furnished with the ability of reversible oxygenation. Extent of hybridization between human adult and canine hemoglobins is highly dependent upon degree of oxygenation of the hemoglobins. A non-linear relationship was found between the extent of hybridization and that of oxygenation, which suggest that a non-straightforward alteration may occur in the quaternary structure of hemoglobin molecule upon the oxygen binding. Mutual ratio of the five hemoglobin fractions, was determined in five adult rats. No significant individual variation was observed for each of the five fractions in all the animals except the one in which one subcomponent was in a lowered level. Author