Hemoglobin Lincoln Park: a betadelta fusion (anti-Lepore) variant with an amino acid deletion in the delta chain-derived segment.
An electrophoretically slow-moving hemoglobin variant was identified in three members of a family originating from Southern Mexico. The variant, Hb Lincoln Park, made up approximately 14% of the total hemoglobin and appeared to have normal stability and functional properties. None of the individuals in whom the abnormal hemoglobin was present was anemic, but each had a mildly elevated reticulocyte count. Structural data suggest that the non-alpha chain of Hb Lincoln Park represents a betadelta gene-fusion product, with normal beta chain structure of the amino-terminal portion of the chain and delta sequences subsequently, the crossover point occurring between animo acid residues 22 and 50. An additional abnormality is the deletion of valine-137, a component of the delta gene-derived segment of the betadelta chain. To account for the development of this abnormal globin chain, a series of intergenic crossovers is proposed; the first, a nonhomologous crossover between the beta and delta genes, presumably gave rise to the betadelta fusion gene; two additional crossovers, one of them unequal, may then have occurred between the same beta and delta genes to produce the amino acid deletion.
D000328:Adult; D000595:Amino Acid Sequence; D002675:Child, Preschool; D002872:Chromosome Deletion; D003434:Crossing Over, Genetic; D005260:Female; D005796:Genes; D006455:Hemoglobins, Abnormal / Q000235:genetics*; D006630:Hispanic or Latino; D006801:Humans; D007526:Isoelectric Point; D046911:Macromolecular Substances; D008297:Male
D006455:Hemoglobins, Abnormal; D046911:Macromolecular Substances