| First Author | Holmes RS | Year | 1976 |
| Journal | Mouse News Lett | Volume | 54 |
| Pages | 32-33 | Mgi Jnum | J:25456 |
| Mgi Id | MGI:73204 | Citation | Holmes RS, et al. (1976) Genetics of mouse Peroxisomal Enzymes. Mouse News Lett 54:32-33 |
| abstractText | Full text of MNL contribution: Research News: 1.0 Genetics of Mouse Peroxisomal Enzymes. (a) Peroxisomes are single membrane bound subcellular organelles occurring predominantly within mice in liver and kidney cells and contain enzymes involved in hydrogen peroxide metabolism: catalase (2H2O2 = 2H2O + 02); alpha-hydroxyacid oxidase (HAOX) (R-CHOH-COO- + 02 = R-CO-COO- + H202); D-amino acid oxidase (DAOX) (D-amino acid + 02 + H20 = R-CO-COO- + NH4 + H202); and urate oxidase (UO) (urate + O2 = unidentified products + H202). (b) HAOX exists as two isozymic forms, termed A and B, which are differentially localized in mouse liver and kidney cells and are controlled by distinct genetic loci (Duley and Holmes, 1974, Genetics 76: 93). The suggested loci symbols are Hao-1 and Hao-2 for the liver (A) and kidney (B) isozymes respectively (Holmes and Duley, 1975, ISOZYMES Volume I (C.L. Markert, ed) page 191), with Hao-la for the allele of normal electrophoretic mobility (all the above strains except NZC/Bl/Wehi) and Hao-1 for the mutant allele of decreased anodal electrophoretic mobility at pH 9.0 (NZC/Bl Wehi). Hao-1 and a showed 5% (4/75) crossover between these loci thereby suggesting the former locus to be localized on chromosome 2. (c) Mouse catalase exists as 5 major forms of activity which are differentially distributed among tissues and subcellular organelles (Holmes and Masters, 1970, FEBS Letters 11:45). These multiple forms have an epigenetic basis of multiplicity (sialic acid binding) (Jones and Masters, 1975, Arch. Biochem. Biophys. 169,7) and are encoded by a single genetic locus (Homles and Duley, 1975, ISOZYMES I, 191). Biochemical evidence indicates that the locus is the structural gene locus for the enzyme. This has been previously designated Cs by Feinstein, with Csa for the allele causing normal activity and electrophoretic mobility (all above strains except Csb) and Csb for the mutant allele causing marked catalase deficiency (Feinstein, Howard, Braun and Seaholm, 1966, Genetics 53, 923) and an altered electrophoretic mobility (Holmes, 1972, FEBS Letters, 24, 161). The Cs locus is located on chromosome 2 since Cs and a showed 17% recombination frequency (Dickerman, Feinstein and Grahn, 1968, J. Heredity 49, 177) and since Cs and Hao-1 showed 7% (5/68) recombination frequency (Holmes and Duley, 1975). The Ce locus (a non structural locus effecting the activity of liver catalase) has been recently shown to be unlinked to Cs (Grieshaber, 1974, J. Heredity 65, 277). (d) The genetics of DAOX has been investigated by Blake and coworkers at the Jackson Laboratory (Blake and Russell, 1972, Science 176: 809; Genetics, 1973, 74, 526; Blake, 1972, Biochem. J. 129, 987) under the enzyme name proline oxidase. DAOX is catalytically active with a number of other D-amino acids besides proline (Biochem. Biophys. Acta 96 (1965) 368) but we will use Blake's suggested gene symbol for DAOX, Pro-1, with Pro-la for the normal allele and Pro-1b for the mutant allele causing DAOX deficiency in PRO/Re mice. We have observed an electrophoretic variant, suggested gene symbol Pro-lc, in NZC/Bl Wehi mice, which is inherited as a normal codominant allele at this locus. |
