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  • 1975-1979  (2)
  • 1955-1959
  • 1910-1914
  • Peromyscus  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Peromyscus alcohol dehydrogenase: Lack of cross-reacting material in enzyme-negative animals (1978)
    Springer
    Biochemical genetics 16 (1978), S. 1093-1105 
    Details
    ISSN: 1573-4927
    Keywords: liver alcohol dehydrogenase ; ADH-negative variant ; monospecific antisera ; enzyme purification ; Peromyscus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Two forms of alcohol dehydrogenase (ADH), coded by allelic genes, have been purified to homogeneity from Peromyscus. Monospecific antisera to the purified enzymes have been raised in rabbits. These antisera fail to detect cross-reacting material in the liver of ADH-negative animals on Ouchterlony plates. Immunotitration of anti-ADH antiserum with ADH in liver extracts from Adh S/Adh S and Adh S/Adh N animals results in identical equivalence points, again suggesting the absence of cross-reacting material coded by the Adh N allele. Over a wide range of anti-ADH antiserum dilutions, radiolabeled protein was not immunoprecipitable from liver extracts of Adh N/Adh N animals. These immunochemical tests, in conjunction with previous studies, suggest that the Adh N allele in Peromyscus does not produce inactive polypeptide in normal levels that bears immunological determinants similar to those of the fast and slow ADH isozymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484530
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Genetic regulation of liver alcohol dehydrogenase in Peromyscus (1978)
    Springer
    Biochemical genetics 16 (1978), S. 443-454 
    Details
    ISSN: 1573-4927
    Keywords: liver alcohol dehydrogenase ; Peromyscus ; genetic polymorphism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Data from genetic crosses of Peromyscus maniculatus and P. polionotus suggest that electrophoretic variants of liver alcohol dehydrogenase are coded by alleles at a single locus. These alleles, designated Adh F , Adh S , and Adh N , determine, respectively, the fast, slow, and not detectable (null) ADH electrophoretic phenotypes. Heterozygotes (Adh F /Adh S ) exhibit three bands on zymograms, suggesting a dimeric subunit structure for the enzyme. However, Adh F /Adh N and Adh S /Adh N animals exhibit a single band, suggesting that the Adh N allele does not produce a polypeptide subunit capable of dimerizing into an active molecule. Fast and slow electrophoretic phenotypes exhibit multiple bands which can be converted into single major fast and slow bands, respectively, upon treatment with oxidized or reduced NAD. Addition of NAD also stabilizes both the fast and slow enzyme to heat inactivation at 60 C for at least 30 min.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484210
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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