Characterization and strain distribution of four alleles at the hemoglobin α-chain structural locus in the mouse
✍ Scribed by Elizabeth S. Russell; Sharon L. Blake; Eleanor C. McFarland
- Publisher
- Springer
- Year
- 1972
- Tongue
- English
- Weight
- 967 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0006-2928
No coin nor oath required. For personal study only.
✦ Synopsis
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 ~ 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 c~T-4 (defining Hba e) and high-intermediate solubility profile. In three inbred strains, a distinct new low-solubility profile, not associated with his-positive ~T-4, was recognized, and mice with this phenotype were classified as Hba d. Implications of observed widely distributed four-allele polymorphism of mouse hemoglobin a-chain structure are discussed.