Abstract
Extract: A premature infant with jaundice was found to have a compensated hemolytic process as evidenced by mild hyperbilirubinemia, a regenerative anemia, and persistence for several months of reticulocytosis, polychromatophilia, and stippled macrocytes. There was no blood loss. When hemoglobins from this family were electrophoresed, the propositus and her mother were found to be heterozygous for an abnormal hemoglobin. The variant hemoglobin, which was 20% of the mother's hemoglobin, had the electrophoretic mobility of hemoglobin S; however, sickle preparations were negative at 24 hr and, in contrast to hemoglobin S, the hemoglobin was soluble in 2.58 M phosphate buffer. The mother's pattern also revealed a faint band running behind A2 and very close to the origin. The distance between this variant and A2 was about the same as the distance between the major variant and A. Such a pattern suggested that the hemoglobin mutation was in the α chain. Examination of the infant's electrophoretic pattern revealed a third variant hemoglobin whose distance from fetal hemoglobin was the same as the distances of the variants in the mother's pattern, which indicated that an abnormal fetal hemoglobin was present. By 7 months of age the infant's electrophoretic pattern was identical with that of her mother and the variant hemoglobin accounted for about 20% of the total.
Since the propositus was a premature infant, structural studies were carried out on the adult variant which was isolated chromatographically from the mother's blood. Analysis of the tryptic peptide chromatogram of the α chain revealed that peptide T-6 was absent; a new peptide was isolated at a lower position on the chromatogram. The amino acid composition of this peptide revealed that the aspartic acid at position 47 was replaced by histidine. Therefore, the mutant hemoglobin was hemoglobin Hasharon (α-47 (CD5) aspartic acid → histidine).
Chromatographically prepared hemoglobin F was hybridized with a similar preparation of the adult hemoglobin Hasharon. After electrophoresis, we found bands corresponding to hemoglobin A and to the fetal hemoglobin Hasharon, as well as the original hemoglobin F and adult hemoglobin Hasharon. There were also two bands which migrated anodal to hemoglobin A which might have been hemoglobin H and hemoglobin Bart's, representing tetramers of the normal β and γ chains. These tetramers may have formed because of the relative instability of the mutant α chains.
Speculation: The marked hemolytic process in this premature infant was dependent on the presence of the fetal form of hemoglobin Hasharon in fetal erythrocytes. Hemolysis resolved as these cells were replaced by adult-type erythrocytes which contained the adult form of hemoglobin Hasharon.
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Levine, R., Lincoln, D., Buchholz, W. et al. Hemoglobin Hasharon in a Premature Infant with Hemolytic Anemia. Pediatr Res 9, 7–11 (1975). https://doi.org/10.1203/00006450-197501000-00002
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DOI: https://doi.org/10.1203/00006450-197501000-00002