Sullivan B
Science. 1967 Sep 15;157(3794):1308-10. doi: 10.1126/science.157.3794.1308.
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.
草腹链蛇血红蛋白具有非常高的氧亲和力，且其氧亲和力对pH的依赖方式不同寻常。蛋白质稀释时氧亲和力略有增加，但玻尔基团的pK值不变。氧化促进血红蛋白聚合，这可通过碘乙酰胺预处理来抑制。与碘乙酰胺反应也会使氧亲和力略有增加，玻尔基团的pK值不变，并使血红素 - 血红素相互作用大幅降低。
