Abstract
THE γ-chain of human foetal haemoglobin (Hb-F) in newborns is chemically heterogeneous1. This conclusion is based on structural analyses of residues 134 to 146 inclusive at the carboxy-terminal end of the γ-chain. This part, termed the γCB-3 peptide, can be isolated by chromatography from the mixture of peptides which is formed when globin F is cleaved with cyanogen bromide. Peptide γCB-3 has the sequence 135 140 145 Val-Thr-Gly(orAla)-Val-Ala-Ser-Ala-Leu-Ser-Ser-Arg-Tyr-His The presence of two types of chain was detected by means of amino-acid analysis of this peptide. Instead of integral numbers of residues for each amino-acid, glycine and alanine gave nonintegral values. Sequence analysis of γCB-3 showed that the third residue of yCB-3 (or residue 136 of the γ-chain) may be occupied either by a glycyl or an alanyl residue. The heterogeneity therefore consists in the presence of two kinds of γ-chains, one of which has a glycyl and the other an alanyl residue at position 136. These are termed the Gγ and Aγ-chains.
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SCHROEDER, W., SHELTON, J., SHELTON, J. et al. World-wide Occurrence of Nonallelic Genes for the y-Chain of Human Foetal Haemoglobin in Newborns. Nature New Biology 240, 273–274 (1972). https://doi.org/10.1038/newbio240273a0
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DOI: https://doi.org/10.1038/newbio240273a0
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