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  • 1
    Electronic Resource
    Electronic Resource
    Genetics and ontogeny of aldehyde dehydrogenase isozymes in the mouse: Localization of Ahd-1 encoding the mitochondrial isozyme on chromosome 4 (1978)
    Springer
    Biochemical genetics 16 (1978), S. 1207-1218 
    Details
    ISSN: 1573-4927
    Keywords: aldehyde dehydrogenase ; mitochondrial isozyme ; genetics ; ontogeny
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Electrophoretic variants for the mitochondrial isozyme of aldehyde dehydrogenase (AHD) have been observed in inbred strains and in Harwell linkage testing stocks of Mus musculus. F1 (LVC×C57BL/Go) mice showed a codominant allele three-banded phenotype, which suggests a dimeric subunit structure (designated AHD-A2). The anodal-migrating supernatant isozyme of AHD was electrophoretically invariant among the 23 inbred strains and stocks examined. The genetic locus encoding AHD-A2 (suggested name Ahd-1) is localized on chromosome 4 and was mapped close to je (jerker) and Gpd-1 (encoding the liver and kidney isozyme of glucose-6-phosphate dehydrogenase). Ontogenetic analyses demonstrated that both AHD isozymes exhibited low activity in late fetal and early neonatal liver and kidney extracts, and reached adult levels within 3 weeks of birth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484541
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  • 2
    Electronic Resource
    Electronic Resource
    Genetic control and ontogeny of microbody enzymes: A review (1978)
    Springer
    Biochemical genetics 16 (1978), S. 171-190 
    Details
    ISSN: 1573-4927
    Keywords: microbody enzymes ; cytoplasmic organelles ; glyoxysomes ; peroxisomes ; microperoxisomes ; ontogeny
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484076
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  • 3
    Electronic Resource
    Electronic Resource
    Genetics of peroxisomal enzymes in the mouse: Nonlinkage of d-amino acid oxidase locus (Dao) to catalase (Cs) and l-α-hydroxyacid oxidase (Hao-1) loci on chromosome 2 (1976)
    Springer
    Biochemical genetics 14 (1976), S. 981-987 
    Details
    ISSN: 1573-4927
    Keywords: d-amino acid oxidase ; peroxisomes ; genetics ; hydroxyacid oxidase ; catalase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract An electrophoretic polymorphism of the peroxisomal enzyme d-amino acid oxidase was observed in NZC strain Mus musculus. F1 (NZC × BALB/c) mice showed a codominant allele two-banded phenotype which is inconsistent with the dimeric subunit structure reported for this enzyme in other species. The enzyme locus (Dao) was shown to segregate independently of Hao-1, encoding the peroxisomal enzyme hydroxyacid oxidase (liver or A4 isozyme). Thus Dao is not linked to previously mapped peroxisomal enzyme loci, Hao-1 and Cs, closely localized on chromosome 2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00485130
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  • 4
    Electronic Resource
    Electronic Resource
    Aldehyde reductase isozymes in the mouse: Evidence for two new loci and localization of Ahr-3 on chromosome 7 (1985)
    Springer
    Biochemical genetics 23 (1985), S. 483-496 
    Details
    ISSN: 1573-4927
    Keywords: mouse ; aldehyde reductase ; isozymes ; hexonate dehydrogenase ; aldose reductase ; gene mapping ; chromosome 7
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Evidence is presented for two new forms of mouse liver and kidney aldehyde reductase activity (designated AHR-3 and AHR-4) resolved using cellulose acetate electrophoresis zymogram techniques and stained by glyceraldehyde and NADPH as substrate and coenzyme, respectively. Activity variants were observed for those isozymes among inbred strains of mice and used in a genetic analyses to support a proposal for two new genetic loci (Ahr-3 and Ah-4) which control the activity phenotype for these isozymes. Segregation analysis indicated that these loci are separately localized on the mouse genome, with Ahr-3 positioned on the distal end of chromosome 7. Liver AHR-2 (or hexonate dehydrogenase) exhibited no detectable phenotypic variation among the 44 inbred strains of mice examined. The AHR-3 and AHR-4 isozymes were readily distinguished from AHR-1 [or aldehyde reductase A2, described previously by Duley and Holmes (Biochem. Genet. 20:1067, 1982)], hexonate dehydrogenase (AHR-2), and alcohol dehydrogenase A2 in terms of their differential substrate, coenzyme, and inhibitor specificities.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00499088
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  • 5
    Electronic Resource
    Electronic Resource
    Genetics and ontogeny of aldehyde dehydrogenase isozymes in the mouse: Evidence for a locus controlling the inducibility of the liver microsomal isozyme (1981)
    Springer
    Biochemical genetics 19 (1981), S. 1223-1236 
    Details
    ISSN: 1573-4927
    Keywords: aldehyde dehydrogenase ; genetics ; ontogeny ; liver microsomes ; mice
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Variation in the inducibility of the liver microsomal isozyme of aldehyde dehydrogenase (designated AHD-Cy) by phenobarbital administration was observed among inbred strains and linkage testing stocks of Mus musculus. The phenotypes were inherited in a normal Mendelian fashion with two alleles showing codominance at a proposed regulatory locus (designated Ahd-3r). Strain variation was also observed for the induction of liver AHD-Cy by 17-β-oestradiol administration to ovarectimized female mice. Moreover, this enzyme was elevated in activity by the administration of high (nonphysiological) levels of progesterone. Development studies showed that the liver and kidney AHD-Cy isozyme exhibited low activities in late-stage fetal and neonatal mice and reached adult levels by approximately 6 weeks of age.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484575
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  • 6
    Electronic Resource
    Electronic Resource
    Genetics and ontogeny of butyryl CoA dehydrogenase in the mouse and linkage of Bcd-1 with Dao-1 (1981)
    Springer
    Biochemical genetics 19 (1981), S. 333-345 
    Details
    ISSN: 1573-4927
    Keywords: butyryl CoA dehydrogenase ; genetics ; ontogeny ; mice
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A zymogram method has been developed for fatty acyl CoA dehydrogenase and used to examine the electrophoretic properties of butyryl CoA dehydrogenase (BCD) from mouse tissues. A single form of BCD is present in extracts of liver, kidney, heart, and intestine. Ontogenetic, tissue distribution, and subcellular fractionation results are consistent with the mitochondrial origin previously reported for this enzyme. A genetic variant for BCD-1 was used to provide evidence for a locus determining the electrophoretic properties of this enzyme (designated Bcd-1), which is linked to Dao-1 (encoding d-amino acid oxidase).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00504278
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  • 7
    Electronic Resource
    Electronic Resource
    Genetics and ontogeny of alcohol dehydrogenase isozymes in the mouse: Evidence for a cis-acting regulator gene (Adt-1) controlling C2 isozyme expression in reproductive tissues and close linkage of Adh-3 and Adt-1 on chromsome 3 (1979)
    Springer
    Biochemical genetics 17 (1979), S. 461-472 
    Details
    ISSN: 1573-4927
    Keywords: alcohol dehydrogenase ; regulator gene ; genetics ; ontogeny
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract An electrophoretic variant previously reported for the stomach isozyme of alcohol dehydrogenase (ADH-C2) in inbred strains of Mus musculus (Holmes, 1977) has been used to localize the gene encoding this enzyme (Adh-3) on chromosome 3 near Va (varitint) (9.6 ± 3.6% recombinants). Genetic variation of ADH-C2 activity in male and female reproductive tissues among inbred strains and Harwell linkage testing stocks was also observed. Reproductive tissue ADH-C2 phenotypes were inherited in a normal Mendelian fashion among F2 progeny of an F1 (LII × C57BL/Go) × C57BL/Go backcross as though controlled by a single cis-acting regulator locus (designated Adt-1) with two alleles: Adt-1 a (presence of ADH-C2) and Adt-1 b (absence or low activity of ADH-C2). No recombinants were observed among 73 progeny or among 13 inbred strains and six Harwell linkage testing stocks of mice, indicating that Adh-3 and Adt-1 are closely linked or identical genes. A single recombinant phenotype was observed in Peru-Coppock mice, suggesting that they are separate genes. Ontogenetic analyses demonstrated that ADH-B2 is present throughout development from late fetal stages in stomach, liver, and kidney; similar results were found for ADH-C2 in developing kidney and stomach extracts, whereas ADH-A2 exhibited high activity in liver extracts after 3 weeks of age in both sexes and in male kidney extracts after 6 weeks.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00498884
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  • 8
    Electronic Resource
    Electronic Resource
    Genetics, ontogeny, and testosterone inducibility of aldehyde oxidase isozymes in the mouse: Evidence for two genetic loci (Aox-1 and Aox-2) closely linked on chromosome 1 (1979)
    Springer
    Biochemical genetics 17 (1979), S. 517-527 
    Details
    ISSN: 1573-4927
    Keywords: aldehyde oxidase genetics ; testosterone inducibility ; ontogeny
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract “Null”-activity and low-activity variants for the liver supernatant isozymes of aldehyde oxidase (designated AOX-1 and AOX-2) were observed in inbred strains and in Harwell linkage testing stocks of Mus musculus. The genetic loci determining the activity of these isozymes (designated Aox-1 and Aox-2, respectively) are closely linked on chromosome 1 near Id-1 (encoding the soluble isozyme of isocitrate dehydrogenase). Linkage data of Aox-1 with Id-1 and Dip-1 (encoding a kidney peptidase) demonstrated that this gene coincides with or is closely linked to Aox (Watson et al., 1972). Ontogenetic analyses demonstrated that liver AOX-1 appeared just before birth and increased in activity during postnatal development, whereas liver AOX-2 was observed only during postnatal development. Adult male livers exhibited higher AOX-1 and AOX-2 activities than adult female livers. Both isozymes were significantly reduced in activity by castration of adult males and increased following testosterone administration to castrated males and normal female mice.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00498887
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  • 9
    Electronic Resource
    Electronic Resource
    Electrophoretic variation of supernatant malate dehydrogenase in marsupials (1974)
    Springer
    Biochemical genetics 11 (1974), S. 25-32 
    Details
    ISSN: 1573-4927
    Keywords: malate dehydrogenase ; isozymes ; marsupials
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Starch gel electrophoresis of supernatant malate dehydrogenase (MDH A2) was performed on erythrocyte samples from 505 individual animals representative of 33 marsupial species. Most species exhibited electrophoretically identical forms of MDH A2 activity with the exception of the grey kangaroos, Trichosurus possums, and bandicoots, thus confirming the phylogenetic relatedness of animals within each group and the conservative nature of this enzyme. Polymorphisms were observed in two of the six species analyzed whose mobilities were non-standard. Allelic isozyme patterns and those from interspecies F1 hybrids between grey kangaroos and other macropods were consistent with a dimeric subunit structure and an autosomal locus (MDH-A) encoding the enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486616
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  • 10
    Electronic Resource
    Electronic Resource
    Biochemical genetics of aldehyde reductase in the mouse: Ahr-1—A new locus linked to the alcohol dehydrogenase gene complex on chromosome 3 (1982)
    Springer
    Biochemical genetics 20 (1982), S. 1067-1083 
    Details
    ISSN: 1573-4927
    Keywords: aldehyde reductase ; alcohol dehydrogenase ; mouse ; chromosome 3
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Electrophoretic and activity variants for a liver aldehyde reductase (AHR-A2) among strains of Mus musculus have been used in genetic analyses to demonstrate close linkage between the locus encoding this enzyme (designated Ahr-1) and the alcohol dehydrogenase gene complex on chromosome 3. No recombinants were observed between Adh-3 (encoding alcohol dehydrogenase C2; ADH-C2) and Ahr-1 among 42 backcross animals. Moreover, linkage disequilibrium between these loci was observed among 58 of 60 strains of mice examined and among seven recombinant inbred strains derived from C57 BL/6J and BALB/c mice. Liver hexonate dehydrogenase (HDH-A) was electrophoretically invariant among the strains examined. Gel filtration analyses demonstrated that AHR-A2 and HDH-A had native molecular weights of approximately 80,000 and 32,000, respectively. Three-banded allozyme patterns for AHR-A2 in CBA/H × castaneus hybrid animals were consistent with a dimeric subunit structure. Comparative substrate and coenzyme specificities for AHR-A2, HDH-A, and ADH-A2 (liver ADH isozyme) were examined. AHR-A2 exhibited a defined specificity toward p-nitrobenzaldehyde as substrate, whereas the other enzymes exhibited broad specificities toward various aliphatic, aromatic, and monosaccharide aldehydes. It is proposed that Ahr-1 is a product of a gene duplication event during mammalian evolution of the primordial mammalian Adh locus and that considerable divergence in catalytic properties has subsequently occurred.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00498933
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