Linkage analyses using biochemical variants in mice. I. Linkage of the hemoglobin beta-chain and glucosephosphate isomerase loci.

Abstract

At least five alleles have been reported at the Hba locus, and each specifies the structure of an α-chain variant of mouse (Mus musculus) hemoglobin. Hba c has proved to be especially useful in genetic linkage experiments and is present in the inbred strains BDP/J, C3H/HeJ, C3HeB/FeJ, DE/J, FL/2ReJ, P/J, SEA/GnJ, SJL/J, SWR/J, ST/bJ, and WB/ReJ. There are three alleles at the hemoglobin β-chain locus, Hbb. Hbb p is found in strain AU/SsJ; other strains have either Hbb s or Hbb d . The β-chains of Hbb d and Hbb p hemoglobins can be alkylated with iodoacetate and have two reactive sites per molecule. The β-chains of Hbb s hemoglobins do not react. If hemoglobins are alkylated before electrophoresis to determine phenotype, alleles at Hbb are codominant. Evidence is presented that the β-chain of Hbb p hemoglobin, like that of Hbb d hemoglobin, has a reactive cysteinyl residue at position β13. Tests for genetic linkage between Hba, Hbb, and 11 other loci showed linkage between glucosephosphate isomerase (Gpi-1) and Hbb with 32±5% recombination. Gpi-1, therefore, is in linkage group I. The Hba locus was not linked with any marker tested.