Abstract
IN the past few years, oxygen equilibria of various normal and abnormal adult human hæmoglobin types have been studied. No differences were observed between normal Hb-A (&α2β2) and the β-chain abnormalities Hb-S (ref. 1), Hb-C (ref. 2) and Hb-E (ref. 3). Investigations of the isolated Hb-A2′ (α2δ2) and its abnormal variant Hb-A2 revealed a considerable increase in oxygen affinity when compared with normal Hb-A (ref. 4). Hb-Lepore, which is composed of normal α-chains and ‘β’ chains being related to the β-chain of Hb-A as well as to the δ-chain of Hb-A2 (ref. 5), showed a high affinity for molecular oxygen similar to that of Hb-A2 (ref. 1). The affinities of the α-chain lacking abnormal hæmoglobin types Hb-H (β4) and Hb-Bart's (γ4) for molecular oxygen were found to be extremely high, while no Bohr effect or hæm–hæm interactions were detectable6,7.
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HUISMAN, T., VAN VEEN, J. Oxygen Equilibria of Red Cell Hæmolysates of Adult Individuals, Heterozygous for Different Rare Abnormal Hæmoglobins. Nature 204, 701 (1964). https://doi.org/10.1038/204701a0
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DOI: https://doi.org/10.1038/204701a0
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