Pawlak A L
Acta Biol Med Ger. 1977;36(5-6):621-4.
Normal values of Bohr effect of oxygenation of partially oxidized hemoglobin A with ferrihemes liganded either with H2O and OH or with CN have been found in the range of pH values from 6.8 to 7.6 in 45 micrometer (Fe)-hemoglobin containing 36--38% of ferrihemes. As the changes of oxygen affinity of Hb A induced by changes of pH are due to the modifications of R state, this quaternary conformation is thought to be unchanged in the studied of R state, this quaternary conformation is thought to be unchanged in the studied forms of partially oxidized hemoglobin. It is suggested that interactions between ferric and ferrous hemes leading to the increased affinity of ferrous hemes to oxygen occur in deoxygenated form of partially oxidized hemoglobin. In partially oxidized hemoglobin with ferric hemes liganded with H2O asymmetry of oxygen binding curves has been noted, which is not observed in forms with ferric hemes liganded with OH ot CN. This shows the effect of ligands of ferric hemes on interactions between chains containing ferric and ferrous hemes.
在含有36%-38%高铁血红素、45微米（铁）血红蛋白中，当高铁血红素与H₂O和OH或与CN结合时，部分氧化血红蛋白A的氧合玻尔效应的正常值在pH值6.8至7.6范围内被发现。由于pH值变化引起的Hb A氧亲和力变化是由于R态的改变，这种四级构象在部分氧化血红蛋白的研究形式中被认为是不变的。有人提出，在部分氧化血红蛋白的脱氧形式中，高铁血红素和亚铁血红素之间的相互作用导致亚铁血红素对氧的亲和力增加。在高铁血红素与H₂O结合的部分氧化血红蛋白中，已注意到氧结合曲线的不对称性，而在高铁血红素与OH或CN结合的形式中未观察到这种情况。这表明高铁血红素的配体对含有高铁血红素和亚铁血红素的链之间的相互作用有影响。
