The oxygen affinity of haemoglobin E

British Journal of Haematology
A May, E R Huehns

Abstract

Oxygen dissociation studies were carried out on haemoglobin E (Hb E) at both high and low haemoglobin concentrations. Oxygen affinities of fresh red cells from three people homozygous for Hb E and from one with Hb E-beta thalassaemia (Hb-E trait/beta-thal trait) were low in three out of four patients studied, while the oxygen affinity of red cells from an individual with Hb-E was normal 2,3-DPG concentration in the fresh cells from the people with homozygous Hb E or Hb-E trait/beta-thal trait which showed low oxygen affinities were elevated sufficiently to account for the shifts observed. When the cells from two of these people with homozygous Hb E were depleted of 2,3-DPG. their oxygen affinities became the same as that of similarly treated normal cells. Pure 'stripped' Hb E in dilute solution behaved identically to Hb A in respect of P50, Bohr shift, haem-haem interaction, and interaction with inorganic phosphate or 2,3-DPG. Hb E, therefore, has the same oxypgen dissociation properties as Hb A both in dilute solution and in the red cell. The low oxygen affinities found in the fresh cells and in whole blood are caused by high 2,3-DPG concentrations within the cell.

References

Jun 1, 1975·British Journal of Haematology·A May, E R Huehns
Jul 1, 1975·British Journal of Haematology·A May, E R Huehns
Nov 1, 1972·The Journal of Clinical Investigation·H F BunnD L Rucknagel
Nov 20, 1969·Annals of the New York Academy of Sciences·P WasiM Pornpatkul
Jun 8, 1968·Nature·A J Bellingham, E R Huehns
Aug 31, 1968·Nature·M F Perutz, H Lehmann
Oct 28, 1967·British Medical Journal·C A WestJ R Ashby

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Citations

Jan 1, 1986·Transactions of the Royal Society of Tropical Medicine and Hygiene·A J VernesC L Diggs
Sep 14, 2010·Blood·Angela AllenDavid Weatherall
Aug 9, 2020·Genes·Janaina Macedo-da-SilvaLivia Rosa-Fernandes
Aug 1, 1987·American Journal of Hematology·N A Lachant

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