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  • genetic variation  (2)
  • 71.55.Fr  (1)
  • 1980-1984  (3)
  • 1960-1964
  • 1935-1939
  • 1920-1924
  • 1
    ISSN: 1432-0630
    Keywords: 78.60.Dg ; 71.55.Fr
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract The annealing behavior of the 0.8 eV luminescence band in undoped semiinsulating GaAs has been investigated. It is found to be fully analogous to that of the AsGa antisite electron-paramagnetic-resonance signal. The radiative recombination of electrons with the doubly ionized AsGa double donor is discussed as the origin for the 0.8 eV band.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 19 (1981), S. 1-14 
    ISSN: 1573-4927
    Keywords: silkworm ; hemolymph β-N-acetylglucosaminidase ; genetic variation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The distribution of insect hemolymph β-N-acetylglucosaminidase was investigated in the silkworm, Bombyx mori. Activity in 115 varieties was 6.92±3.22 units/ml, ranging from 1.4 to 17.0 units/ml. No enzyme-deficient individuals were observed. By selecting individuals showing either high or low enzyme activities, homozygotes were separated with activities varying 10-fold between isolates. No differences in activity of α-mannosidase and β-galactosidase were observed. Thus, it appears that high- or low-enzyme silkworms (High or Low lines) shared the same genetic background except for the gene concerning the activity of β-N-acetylglucosaminidase. Studies on the heredity of the enzyme indicated that the synthesis of the enzyme protein was controlled by an autosomal allele. Examination by immunotitration and CM52-cellulose column chromatography revealed that the difference in activity between High and Low lines was due to the amount of the active enzyme, but not to an endogeneous activator or inhibitor. Furthermore, there was no isozymic difference in β-N-acetylglucosaminidase. Slab gel electrophoresis on polyacrylamide showed a species of enzyme (A) that stained more intensely in the High line. For the second species of enzyme (B), the converse was true. This evidence suggests that enzyme levels in hemolymph are under the control of a gene affording association of enzyme subunits to the active enzyme molecule.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 21 (1983), S. 713-724 
    ISSN: 1573-4927
    Keywords: insect α-mannosidase ; genetic variation ; enzymic characterization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The genetics of hemolymph α-mannosidase was investigated in the silkworm, Bombyx mori. By selecting individuals showing either high or low enzyme activities, homozygotes were separated, with activities varying about five-fold. No differences in the activities of β-galactosidase and β-N-acetylglucosaminidase were observed. Thus, it seems that high- and low-enzyme silkworms (High and Low lines) share the same genetic background except for the gene concerning the activity of α-mannosidase. The synthesis of the enzyme is controlled by an autosomal allele. Furthermore, expression of the gene varies from tissue to tissue, and there is no correlation between enzyme activity and growth rate. The difference in activity between High and Low lines is due to the amount of active enzyme, not to an endogeneous activator or inhibitor. There was no isozymic difference in α-mannosidase.
    Type of Medium: Electronic Resource
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