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The Oxygen Affinity of Haemoglobin E
Author(s) -
May A.,
Huehns E. R.
Publication year - 1975
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1975.tb00532.x
Subject(s) - bohr effect , oxygen , affinities , chemistry , oxygen–haemoglobin dissociation curve , p50 , red cell , hemoglobin , trait , sickle cell trait , dissociation (chemistry) , biochemistry , medicine , gene , organic chemistry , computer science , transcription factor , programming language , disease
S ummary . 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‐β thalassaemia (Hb‐E trait/β‐thai trait) were low in three out of four patients studied, while the oxygen affinity of red cells from an individual with Hb‐E trait was normal. 2, 3‐DPG concentration in the fresh cells from the people with homozygous Hb E or Hb‐E trait/β‐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 P 50 , Bohr shift, haem‐haem interaction, and interaction with inorganic phosphate or 2, 3‐DPG. Hb E, therefore, has the same oxygen 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.