Abstract
AT first, the γ chain of human haemoglobin seemed to be a constant chemical species1, but Schroeder et al. showed that two or possibly four of the γ chain loci which control the synthesis of the two types of chains, Aγ and Bγ, are active in new born infants2. The two chains differ only at position 136, where Aγ has alanine and Gγ has glycine. Thus although they are inseparable by chromatography and electrophoresis, their relative concentrations can be estimated from the ratio of these two amino-acids in the third and last peptide (γCB3) produced by hydrolysis of the chains by cyanogen bromide. Schroeder et al. studied the variations in the levels of these two chains during the normal ontogenic development and in several cases of hereditary persistence of foetal haemoglobin (HPHF) and β thalassaemias3–5. We have studied the γ chains synthesized in different types of acquired anaemia with increased amounts of foetal haemoglobin, of which haemoglobin F constitutes between 1 and 15%. Such anaemias include refractory anaemias with excess myeloblasts (RAEM), acquired sideroblastic idiopathic anaemias (ASIA), idiopathic aplastic anaemias and some varieties of leukaemias, especially juvenile myeloid leukaemias (JML).
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References
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ROSA, J., BEUZARD, Y., BRUN, B. et al. Evidence for Various Types of Synthesis of Human γ Chains of Haemoglobin in Acquired Haematological Disorders. Nature New Biology 233, 111–113 (1971). https://doi.org/10.1038/newbio233111a0
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DOI: https://doi.org/10.1038/newbio233111a0
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