Abstract
INGRAM and Hunt1–3 reported that normal human hæmoglobin (hæmoglobin A) differs from certain of the abnormal human hæmoglobins by a single amino-acid in the primary structure of the β-chains of the globin of these proteins. The peptides from a tryptic digest of hæmoglobin A and hæmoglobin S were visibly identical except for one peptide (peptide 4) in which a glutamyl residue in hæmoglobin A was replaced by a valyl residue in hæmoglobin S. We have isolated an abnormal peptide in hæmoglobin G 4 and have compared it to similar peptides obtained from hæmoglobins A and S. By amino-acid analysis and sequence determinations, it is evident that hæmoglobin G possesses an abnormal amino-acid in the tryptic peptide number 4 of Ingram. The sequences determined for the tryptic peptides from hæmoglobins A and G are: Hæmoglobin A: Val.His.Leu.Thr.Pro.Glu.Glu.Lys. G: Val.His.Leu.Thr.Pro.Glu.Gly.Lys.
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HILL, R., SCHWARTZ, H. A Chemical Abnormality in Hæmoglobin G . Nature 184, 641–642 (1959). https://doi.org/10.1038/184641a0
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DOI: https://doi.org/10.1038/184641a0
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