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  • 1
    Electronic Resource
    Electronic Resource
    Biochemical genetic markers of squirrel monkeys and their use for pedigree validation (1990)
    Springer
    Biochemical genetics 28 (1990), S. 41-56 
    Details
    ISSN: 1573-4927
    Keywords: isozymes ; polymorphisms ; paternity ; maternity ; pedigree ; Saimiri
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Family data for 14 biochemical genetic markers of squirrel monkeys (genusSaimiri) were derived from 73 pedigreed progeny and both parents of each, as well as from 16 additional progeny and one parent of each. The data for each marker and the phenotypic patterns were consistent with autosomal codominant inheritance. It was concluded from the genetic marker data that the pedigree records of seven progeny were incorrect. Retrospective investigations of colony records followed by typing of animals that might possibly have been a parent enabled five of the pedigree records to be corrected. Although five of the pedigree errors were cases of mistaken paternity, the other two apparently were the consequence of infant swapping between dams shortly after birth. Because squirrel monkeys exhibit a high degree of allomaternal behavior, infant swapping between dams may occur more frequently than in many other nonhuman primate species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00554820
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  • 2
    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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  • 3
    Electronic Resource
    Electronic Resource
    Biochemical genetics of alcohol dehydrogenase isozymes in the gray short-tailed opossum (Monodelphis domestica) (1992)
    Springer
    Biochemical genetics 30 (1992), S. 215-231 
    Details
    ISSN: 1573-4927
    Keywords: marsupial ; opossum ; alcohol dehydrogenase ; isozymes ; genetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Polyacrylamide gel-isoelectric focusing (PAGE-IEF) methods were used to examine the multiplicity, tissue distribution, and biochemical genetics of alcohol dehydrogenase (ADH) isozymes among gray short-tailed opossums (Monodelphis domestica). Seven ADH isozymes were resolved and distinguished on the basis of their isoelectric points, tissue distributions, and substrate and inhibitor specificities. ADH1 and ADH2 exhibited Class I properties and were observed in liver (and intestine) extracts. ADH3, ADH4, and ADH5 showed “high-K m ” (possibly Class IV) properties, with ADH3 and ADH4 exhibiting high activity in cornea, ear, stomach, and esophagus extracts. ADH6 and ADH7 exhibited Class III properties, including activities as formaldehyde dehydrogenases, with each showing different tissue distribution characteristics; ADH6 was widely distributed, and ADH7 was restricted to prostate extracts. An additional form of formaldehyde dehydrogenase (FDH) was observed, which was inactive with hexenol and ethanol as substrates. Isoelectric point variants were observed for ADH3 (three forms) and for ADH4 (two forms), and the inheritance of ADH3 was studied in 15 families ofM. domestica. The data were consistent with codominant inheritance of two alleles (ADH3*A andADH3*B) at a single autosomal locus (designatedADH3) and with a model involving a dimeric ADH isozyme: ADH3 (γ2 isozyme, forming three dimers designated γ 2 1 , γ1 γ2, and γ 2 2 in heterozygous individuals).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02396213
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  • 4
    Electronic Resource
    Electronic Resource
    Biochemical genetics of alcohol dehydrogenase isozymes in the gray short-tailed opossum (Monodelphis domestica) (1992)
    Springer
    Biochemical genetics 30 (1992), S. 215-231 
    Details
    ISSN: 1573-4927
    Keywords: marsupial ; opossum ; alcohol dehydrogenase ; isozymes ; genetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Polyacrylamide gel-isoelectric focusing (PAGE-IEF) methods were used to examine the multiplicity, tissue distribution, and biochemical genetics of alcohol dehydrogenase (ADH) isozymes among gray short-tailed opossums (Monodelphis domestica). Seven ADH isozymes were resolved and distinguished on the basis of their isoelectric points, tissue distributions, and substrate and inhibitor specificities. ADH1 and ADH2 exhibited Class I properties and were observed in liver (and intestine) extracts. ADH3, ADH4, and ADH5 showed “high-K m ” (possibly Class IV) properties, with ADH3 and ADH4 exhibiting high activity in cornea, ear, stomach, and esophagus extracts. ADH6 and ADH7 exhibited Class III properties, including activities as formaldehyde dehydrogenases, with each showing different tissue distribution characteristics; ADH6 was widely distributed, and ADH7 was restricted to prostate extracts. An additional form of formaldehyde dehydrogenase (FDH) was observed, which was inactive with hexenol and ethanol as substrates. Isoelectric point variants were observed for ADH3 (three forms) and for ADH4 (two forms), and the inheritance of ADH3 was studied in 15 families ofM. domestica. The data were consistent with codominant inheritance of two alleles (ADH3*A andADH3*B) at a single autosomal locus (designatedADH3) and with a model involving a dimeric ADH isozyme: ADH3 (γ2 isozyme, forming three dimers designated γ 2 1 , γ1 γ2, and γ 2 2 in heterozygous individuals).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00553751
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  • 5
    Electronic Resource
    Electronic Resource
    Aldehyde dehydrogenase (ALDH) isozymes in the gray short-tailed opossum (Monodelphis domestica): Tissue and subcellular distribution and biochemical genetics of ALDH3 (1991)
    Springer
    Biochemical genetics 29 (1991), S. 163-175 
    Details
    ISSN: 1573-4927
    Keywords: aldehyde dehydrogenase ; isozymes ; opossum ; genetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Polyacrylamide gel isoelectric focusing (PAGE-IEF), cellulose acetate electrophoresis, and histochemical techniques were used to examine the tissue and subcellular distribution, genetics and biochemical properties of aldehyde dehydrogenase (ALDH) isozymes in a didelphid marsupial, the gray short-tail opossum (Monodelphis domestica). At least 14 zones of activity were resolved by PAGE-IEF and divided into five isozyme groups and three ALDH classes, based upon comparisons with properties previously reported for human, baboon, rat, and mouse ALDHs. Opossum liver ALDHs were distributed among cytosol (ALDHs 1 and 5) and large granular (mitochondrial) fractions (ALDHs 2 and 5). Similarly, kidney ALDHs were distributed between the cytosol (ALDH5) and the mitochondrial fractions (ALDHs 2, 4, and 5), whereas a major isozyme (ALDH3), found in high activity in cornea, esophagus, ear pinna, tail, and stomach extracts, was localized predominantly in the cytosol fraction. Phenotypic variants of the latter enzyme were shown to be inherited in a normal Mendelian fashion, with two alleles at a single locus (ALDH3) showing codominant expression. The data provided evidence for genetic identity of corneal, ear pinna, tail, and stomach ALDH3 and supported biochemical evidence from other mammalian species that this enzyme has a dimeric subunit structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00554209
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  • 6
    Electronic Resource
    Electronic Resource
    Aldehyde dehydrogenase (ALDH) isozymes in the gray short-tailed opossum (Monodelphis domestica): Tissue and subcellular distribution and biochemical genetics of ALDH3 (1991)
    Springer
    Biochemical genetics 29 (1991), S. 163-175 
    Details
    ISSN: 1573-4927
    Keywords: aldehyde dehydrogenase ; isozymes ; opossum ; genetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Polyacrylamide gel isoelectric focusing (PAGE-IEF), cellulose acetate electrophoresis, and histochemical techniques were used to examine the tissue and subcellular distribution, genetics and biochemical properties of aldehyde dehydrogenase (ALDH) isozymes in a didelphid marsupial, the gray short-tail opossum (Monodelphis domestica). At least 14 zones of activity were resolved by PAGE-IEF and divided into five isozyme groups and three ALDH classes, based upon comparisons with properties previously reported for human, baboon, rat, and mouse ALDHs. Opossum liver ALDHs were distributed among cytosol (ALDHs 1 and 5) and large granular (mitochondrial) fractions (ALDHs 2 and 5). Similarly, kidney ALDHs were distributed between the cytosol (ALDH5) and the mitochondrial fractions (ALDHs 2, 4, and 5), whereas a major isozyme (ALDH3), found in high activity in cornea, esophagus, ear pinna, tail, and stomach extracts, was localized predominantly in the cytosol fraction. Phenotypic variants of the latter enzyme were shown to be inherited in a normal Mendelian fashion, with two alleles at a single locus (ALDH3) showing codominant expression. The data provided evidence for genetic identity of corneal, ear pinna, tail, and stomach ALDH3 and supported biochemical evidence from other mammalian species that this enzyme has a dimeric subunit structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02401810
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