Abstract
EVIDENCE has been presented in a previous investigation1 that the normally occurring minor hæmoglobin component A2 has a considerably higher affinity for oxygen than normal Hb–A. The Hb–A2 preparations, which were isolated by carboxymethyl-cellulose (CMC) chromatography2, however, contained relatively large quantities (up to 20 per cent) ferri–Hb or ferri–Hb derivatives. In the work reported here we redetermined, therefore, the oxygen equilibria of normal Hb–A0 and Hb–A2, both being isolated as oxyhæmoglobin without notable oxidation to ferri-hæmoglobin derivatives. The abnormal variant of Hb–A2, known as Hb–A21 or Hb–B2 (ref. 3), has also been included in this work.
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HUISMAN, T., DOZY, A., NECHTMAN, C. et al. Oxygen Equilibrium of Hæmoglobin A2 and Its Variant Hæmoglobin A21, (or B2). Nature 195, 1109–1110 (1962). https://doi.org/10.1038/1951109a0
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DOI: https://doi.org/10.1038/1951109a0
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