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  • Articles  (2)
  • Articles: DFG German National Licenses  (2)
  • Biology  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Nature of the heterozygote blood catalase in a hypocatalasemic mouse mutant (1968)
    Springer
    Biochemical genetics 1 (1968), S. 277-285 
    Details
    ISSN: 1573-4927
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The blood catalase of a hypocatalasemic mouse mutant has been compared with that of the wild-type (normal) animal and with that of the heterozygote. Comparison is on the basis of stability to heat and to urea. Electrophoretic evidence is of no value, because all forms tested show the same mobility. Because the heterozygote heat and urea inactivation curves differ from those of the two parental forms, and because the curves are smoothly S-shaped, with no shoulders or other irregularities, it is suggested that this heterozygote produces only a single molecular form of the enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00485182
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular location of the genetic lesion in the acatalasemic mouse (1972)
    Springer
    Biochemical genetics 6 (1972), S. 263-273 
    Details
    ISSN: 1573-4927
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Antibody to normal mouse catalase will stabilize blood and liver catalase of the acatalasemic mouse against a variety of agents which damage protein tertiary structure (urea, guanidine, trypsin) but not against agents which affect the heme group (azide, hydroxylamine). The antibody will also stabilize catalase against inhibition by 3-amino 1,2,4-triazole (AT), the specific site of action of which is known. The antibody is able also to protect normal mouse catalase from urea denaturation, but it is without effect on AT inhibition of normal catalase. A hypothesis is proposed which explains these results and which helps localize the site of the mutation on the catalase molecule.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486120
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    Paper (German National Licenses)
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