Churchill Hospital
Publishes on Hemoglobinopathies and Related Disorders, Hemoglobin structure and function, Animal Nutrition and Physiology. 105 papers and 4.1k citations.
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Abstract Excellent resolution of human and baboon globin chains may be obtained by HPLC on a Vydac large-pore C4 column. The procedure is rapid and uses a gradient between aqueous trifluoroacetic acid and trifluoroacetic acid in acetonitrile. The common human γ chains are easily separable from each other as are some α- and β-chain variants from the normal chains and from each other.
A sequence with a specific residue at each position was proposed for the γ chain of human fetal hemoglobin by Schroeder et al. (1) after a study in which hemoglobin from a number of individual infants was used. We have now examined in part the fetal hemoglobin components of 17 additional infants and have observed that position 136 of the γ chain may be occupied not only by a glycyl residue, as previously reported, but also by an alanyl residue.
The 146 amino acid residues of the γ chain of human fetal hemoglobin have been placed in sequence. The fetal hemoglobin for this investigation was isolated chromatographically from umbilical cord blood. The α and γ chains were separated prior to the determination of sequence. For the determination of the sequence, peptides were produced by individual hydrolyses with trypsin, chymotrypsin, or pepsin. The sequence of the individual peptides was determined largely through the application of the Edman degradation. The differences between the γ chains of human fetal hemoglobin and the β chains of human adult hemoglobin are responsible for the differences in the properties of the two molecules.