Multiple hemoglobin alpha-chains in the sika deer (Cervus nippon).

Investigation of the hemoglobin alpha-chains of an Asiatic deer, the sika (Cervus nippon), was prompted by the heterogenity of alpha-chain gene loci in the Virginia white-tailed deer (Odocoileus virginianus). Although electrophoresis of hemoglobin chains from 10 sika revealed only a single alpha-chain band, peptide mapping demonstrated variations in the alpha-TPIII and alpha-TPIV peptides. Substitutions at positions 15, 20, and 22 produced a minimum of five alpha-chains; two possible additional chains could noy be proven because of inseparability of the whole alpha-chains. The most common chain contains Asp-15, Lys-20 and Pro-22 but in other chains glycine is present at position 15, Asx at position 20, and either serine or Asx at position 22. The probable explanation for the large number of alpha-chains is gene duplication which may have been produced by breedings between subspecies from different geographical areas. Comparison with the alpha-chain structure of the white-tailed deer suggests that the sika may have evolved from the lineage which produced the white tailed-deer after the alpha-chain genes of the latter species had duplicated. In addition, these data provide further examples of the unusual variability of this portion of the alpha-chain.