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  • L-alanosine  (1)
  • Mutagen sensitivity  (1)
  • privatization  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    European journal of law and economics 3 (1996), S. 39-60 
    ISSN: 1572-9990
    Keywords: liability ; privatization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Law , Economics
    Notes: Abstract The legacy of severe environmental degradation inherited by the new Central and Eastern European (CEE) economies requires liability reform to aid the cleanup of existing pollution sources and create incentives for future environmental risk reduction. The paper analyzes a host of liability approaches to meet these goals, given economic and institutional characteristics specific to the CEE nations, and explores the impact of environmental liability rules on privatization and foreign investment. A principal conclusion of the analysis is that, for a host of efficiency-based reasons, liability should not be retroactively applied to the new owners of privatized firms. Also, the paper advocates the use of national liability funds to finance the cost of existing liabilities, while highlighting dangers associated with their use. In addition to the desirability of alternative privatization mechanisms, the paper also analyzes altemative liability rules to govern prospective environmental hazards.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1617-4623
    Keywords: Deoxyribonuclease ; Mitochondria ; Mutagen sensitivity ; Drosophila ; mus308
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The mus308 mutants of Drosophila have previously been demonstrated to be defective in an enzyme that is designated Nuclease 3 (Boyd et al. 1990b). In this study that enzyme is shown to be present in mitochondria of both wild-type flies and embryos. Since the mus308 mutants are hypersensitive to DNA crosslinking agents, Nuclease 3 is potentially required for resistance of the mitochondrial genome to such agents. In support of this hypothesis, electron microscopic studies of mus308 mutant flies that had been exposed to nitrogen mustard revealed an increased frequency of mitochondrial abnormalities. Further investigation of the defect at the enzymological level revealed that the mutants possess a new nuclease activity that is apparently a modified form of the wild-type protein. In the earlier study, enzyme extracts from mus308 mutants were found to lack an enzyme with a pl of approximately 6.2. More precisely defined assay conditions in this study revealed the appearance of a new nuclease activity with a higher pI in extracts from mutants. This observation, together with the finding that only the normal enzyme form is present in heterozygous individuals, supports the hypothesis that the mus308 locus is not the structural gene for the enzyme. Rather, the mus308 gene product is necessary for Nuclease 3 to assume the lower pI. Nuclease 3 has been partially purified and characterized from wild-type embryos. Its activity is stimulated by Mg++ and ATP. Optimum activity is found at a pH of 5.5 and a NaCl concentration of 50–100 mM. Nuclease 3 exhibits a temperature optimum of 42°C and is insensitive to N-ethylmaleimide. The enzyme is probably membrane-associated because it exhibits a strong tendency to aggregate and detergent is required for full solubilization.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-0646
    Keywords: phase II ; L-alanosine ; breast cancer
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
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