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  • Drosophila melanogaster
  • Springer  (9)
  • American Meteorological Society
  • Blackwell Publishing Ltd
  • International Union of Crystallography
  • Springer Nature
  • 2015-2019
  • 1985-1989
  • 1975-1979
  • 1970-1974  (9)
  • 1960-1964
  • 1950-1954
  • 1974  (9)
Collection
Keywords
Publisher
  • Springer  (9)
  • American Meteorological Society
  • Blackwell Publishing Ltd
  • International Union of Crystallography
  • Springer Nature
Years
  • 2015-2019
  • 1985-1989
  • 1975-1979
  • 1970-1974  (9)
  • 1960-1964
    • +
Year
  • 1
    Electronic Resource
    Electronic Resource
    Properties of alcohol dehydrogenase isozymes in a strain of Drosophila melanogaster homozygous for the Adh-slow allele (1974)
    Springer
    Biochemical genetics 11 (1974), S. 167-175 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; alcohol dehydrogenase ; isozymes ; conformers
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Two isozymes of alcohol dehydrogenase from Drosophila melanogaster homozygous for the Adh-slow allele have been separated by isoelectric focusing. The isozymes differ in their temperature optima, temperature stabilities, specific activities, and at least one of their Michaelis constants. They are immunologically identical. Evidence is presented that NAD may partially convert one isozyme into another. The possible nature of these isozymic differences is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00485772
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  • 2
    Electronic Resource
    Electronic Resource
    Phenol oxidase activity and the Lozenge locus of Drosophila melanogaster (1974)
    Springer
    Biochemical genetics 11 (1974), S. 359-365 
    Details
    ISSN: 1573-4927
    Keywords: lozenge ; phenol oxidase ; Drosophila melanogaster ; tyrosinase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract We have found that the phenol oxidase activity in 50-hr Drosophila melanogaster pupae is much greater than that of adult flies. The mutants lz and lz g have all of the phenol oxidase components present in wild type, whereas the mutant tyr-1 has all of the wild-type components but the activity of each component is greatly reduced in comparison with wild-type activity. The newly discovered lozenge allele, lz rfg, lacks all phenol oxidase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486409
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  • 3
    Electronic Resource
    Electronic Resource
    Alkaline phosphatase of Drosophila melanogaster. III. Tyrosine-O-phosphate as substrate (1974)
    Springer
    Biochemical genetics 11 (1974), S. 177-180 
    Details
    ISSN: 1573-4927
    Keywords: alkaline phosphatase ; Drosophila melanogaster ; tyrosine-O-phosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Tyrosine-O-phosphate was used as a substrate for two allelic forms (APH-4 and-6) of alkaline phosphatase of late third instar larvae of Drosophila melanogaster. Two findings of particular interest are (1) lack of inhibition by 1mm inorganic phosphate and (2) severe substrate inhibition. The accumulated evidence that, in vivo, alkaline phosphatase catalyzes the conversion of tyrosine-O-phosphate into tyrosine, which is then utilized for puparium formation, is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00485773
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  • 4
    Electronic Resource
    Electronic Resource
    Properties of genetically polymorphic isozymes of alcohol dehydrogenase in Drosophila melanogaster (1974)
    Springer
    Biochemical genetics 11 (1974), S. 141-153 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; alcohol dehydrogenase ; isozymes ; allozymes ; polymorphism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Studies of the isozymes produced by alternative alleles at the alcohol dehydrogenase locus of Drosophila melanogaster indicate that the ADH F enzyme is more active but less stable than the ADHS enzyme. The difference in stability is manifested in the responses to various conditions of temperature, pH, and protein concentration. The two enzymes also appear to differ in their substrate specificities. It is clear that the differences of primary structure involved in the ADH polymorphism can have profound effects on the biological activity of the molecule.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00485770
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  • 5
    Electronic Resource
    Electronic Resource
    The relative quantities and catalytic activities of enzymes produced by alleles at the alcohol dehydrogenase locus in Drosophila melanogaster (1974)
    Springer
    Biochemical genetics 11 (1974), S. 155-165 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; alcohol dehydrogenase ; isozymes ; enzyme kinetics ; polymorphism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract We have examined the kinetic properties of enzymes produced by the electrophoretically fast (F) and slow (S) alleles at the alcohol dehydrogenase locus in a polymorphic laboratory population of Drosophila melanogaster. The product of the F allele has approximately twice the specific activity of the product of the S allele. We have estimated four Michaelis constants (K ethanol, K NAD, K′ethanol, and K′NAD) and have found no significant difference between the major (ADH-5) isozyme produced by homozygotes for the two alleles. The relative amounts of enzyme produced by the homozygotes were estimated by the method of Laurell (1966), and again no significant differences were found. It appears that the difference in specific activities can be explained solely in terms of relative catalytic efficiency. In a series of laboratory stocks, those fixed for the F allele tend to produce more enzyme than those fixed for the S allele. These observations do not support the view that the alleles are selectively equivalent.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00485771
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  • 6
    Electronic Resource
    Electronic Resource
    Genetics of esterases in Drosophila. III. Influence of different chromosomes on esterase pattern in Drosophila (1974)
    Springer
    Biochemical genetics 12 (1974), S. 9-24 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; Drosophila simulans ; interspecific hybrids ; esterases ; regulation by X chromosome in Drosophila
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The present report presents the results of starch and polyacrylamide gel electrophoretic studies of the influence of the X chromosome on the expression of esterase-6 in D. melanogaster × D. simulans hybrids heterozygous for locus Est-6 as well as studies of the influence of autosomes on esterase expression in Drosophila of the virilis group. A differential expression of esterase-6 has been detected in D. melanogaster × D. simulans hybrid males. A differential decrease in the activity of esterase-6 (both F and S allozymes) derived from D. melanogaster has been noted. In hybrid females, the activity of parental esterases is the same. It is suggested that the X chromosome regulates the expression of esterase-6 in D. melanogaster. Analysis of individuals obtained in different schemes of crosses between different species of Drosophila of the virilis group by use of stocks marked with mutations in various chromosomes indicates that other autosomes (in particular, autosomes 4 and 5) also influence the phenotypic expression of esterases (which are controlled by genes located on the second chromosome).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00487524
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  • 7
    Electronic Resource
    Electronic Resource
    Alcohol dehydrogenase in Drosophila melanogaster: Activity variation in natural populations (1974)
    Springer
    Biochemical genetics 12 (1974), S. 449-458 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; alcohol dehydrogenase ; protein polymorphism ; allozymes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A natural population of Drosophila melanogaster was examined for activity variation in the polymorphic enzyme alcohol dehydrogenase. The overall mean activity of the ADH-F strains proved to be approximately twice that of the ADH-S strains. Within each of the two electrophoretic classes, there was a wide spread of activity values and some overlap in activity between the classes. This variation should be taken into account when discussing the functional significance of the electrophoretically detectable polymorphism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486062
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  • 8
    Electronic Resource
    Electronic Resource
    Genetic control of activity, preening, and the response to a shadow stimulus inDrosophila melanogaster (1974)
    Springer
    Behavior genetics 4 (1974), S. 317-329 
    Details
    ISSN: 1573-3297
    Keywords: genetics ; activity ; preening ; stimulation ; Drosophila melanogaster
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Psychology
    Notes: Abstract Spontaneous locomotor activity, preening and the change in frequency of each in response to a shadow have been studied in Drosophila melanogaster by means of a time-sampling technique. The genetic control of these four behaviors was elucidated by application of biometrical genetic analysis. The genetic architecture for spontaneous activity indicated a history of natural selection for comparatively high activity. There was a tendency for both activity and preening to decrease in response to shadow stimulation. The genetic control indicates that this form of reaction is advantageous and suggests a relation to the avoidance of predation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01066153
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  • 9
    Electronic Resource
    Electronic Resource
    Activity and sexual behavior of neurological mutants inDrosophila melanogaster (1974)
    Springer
    Behavior genetics 4 (1974), S. 227-235 
    Details
    ISSN: 1573-3297
    Keywords: Drosophila melanogaster ; activity ; sexual behavior ; mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Psychology
    Notes: Abstract The neurological mutantsHyperkinetic andShaker inDrosophila melanogaster differ quantitatively in their patterns of behavior from the wild type. Differences are apparent during the pre-imaginal stages, when the mutants show a reduction in the rate of larval feeding. Adult mutants exhibit a lower rate of sustained locomotor activity; they frequently make jumps or short flights and then fall over. UnlikeShaker flies, theHyperkinetic mutants have difficulty in regaining equilibrium after falling over and thrash about in a disorganized manner. The mutants differ significantly in mean duration of dyskinesis.Shaker mutant males do not differ significantly in mating speed from wild type.Hyperkinetic males tend to switch rapidly from one behavior to another and show a marked reduction in mating speed caused by frequent loss of contact with the females during courtship.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01074156
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