Hemoglobin Beta chain structural variation in mice: evolutionary and functional implications
- PMID: 5085986
- DOI: 10.1126/science.178.4063.873
Hemoglobin Beta chain structural variation in mice: evolutionary and functional implications
Abstract
The Hbb(d) allele at the hemoglobin beta chain locus of Mus musculus is composed of two linked genes, coding for structurally different beta chains, betadmin and betadmaj. Mus caroli has only one beta chain, which combines structural features of both betadmin and betadmaj and thus may be a Lepore type of beta chain. Sequence data suggest that selection may have been important in the evolution of the mouse beta chains.
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