Oxygenation properties of snake hemoglobin.

Natrix taxispilota hemoglobin has a very high oxygen affinity which depends upon pH in an unusual manner. The oxygen affinity increases slightly upon protein dilution, but the pK's of the Bohr groups are unchanged. Oxidation promotes hemoglobin polymerization, which can be inhibited by prior treatment with iodoacetamide. Reaction with iodoacetamide also causes a slight increase in the oxygen affinity, no change in the pK's of the Bohr groups, and a drastic reduction in heme-heme interaction.