LINKAGE ANALYSES USING BIOCHEMICAL VARIANTS IN MICE .I. LINKAGE OF HEMOGLOBIN BETA-CHAIN AND GLUCOSEPHOSPHATE ISOMERASE LOCI

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. Hbac 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. Hbbp is found in strain AU/SsJ; other strains have either Hbbs or Hbbd. The β-chains of Hbbd and Hbbp hemoglobins can be alkylated with iodoacetate and have two reactive sites per molecule. The β-chains of Hbbs 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 Hbbp hemoglobin, like that of Hbbd 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. © 1969 Plenum Publishing Corporation.