Abstract
In a survey of mice from 40 inbred strains, largely previously untested, four alleles were distinguished at the Hba locus, determining structure of adult mouse hemoglobin α chain. This finding supports and extends previous sequence studies by others. Methods are given by which each phenotype was characterized by its solubility profile at varying pH and by its chromatography pattern. Concordance was complete between histidine-positive αT-4 (defining Hba c) and high-intermediate solubility profile. In three inbred strains, a distinct new low-solubility profile, not associated with his-positive αT-4, was recognized, and mice with this phenotype were classified as Hba d. Implications of observed widely distributed four-allele polymorphism of mouse hemoglobin α-chain structure are discussed.
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This investigation was supported in part by NIH research grant CA-01074 from the National Cancer Institute and in part by the Virginia and D. K. Ludwig Foundation. The Jackson Laboratory is fully accredited by the American Association for Accreditation of Laboratory Animal Care.
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Russell, E.S., Blake, S.L. & McFarland, E.C. Characterization and strain distribution of four alleles at the hemoglobin α-chain structural locus in the mouse. Biochem Genet 7, 313–330 (1972). https://doi.org/10.1007/BF00484831
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DOI: https://doi.org/10.1007/BF00484831