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  • 1995-1999  (4)
  • 1955-1959
  • 1890-1899
  • 1999  (4)
  • genetic engineering
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Years
  • 1995-1999  (4)
  • 1955-1959
  • 1890-1899
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    The journal of ethics 3 (1999), S. 51-71 
    ISSN: 1572-8609
    Keywords: biotechnology ; cloning ; ethics of biotechnology ; ethics of cloning ; ethics of human cloning ; ethics for reproductive technology ; genetic engineering ; human cloning ; religious ethics ; reproductive technology ; secular ethics ; social ethics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Philosophy
    Notes: Abstract The advent of cloning animals has created a maelstrom of social concern about the “ethical issues” associated with the possibility of cloning humans. When the “ethical concerns” are clearly examined, however, many of them turn out to be less matters of rational ethics than knee-jerk emotion, religious bias, or fear of that which is not understood. Three categories of real and spurious ethical concerns are presented and discussed: 1) that cloning is intrinsically wrong, 2) that cloning must lead to bad consequences, and 3) that cloning harms the organism generated. The need for a rational ethical framework for discussing biotechnological advances is presented and defended.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1572-9788
    Keywords: transgenic carnation ; genetic engineering ; microprojectile bombardment ; stable transformation ; kanamycin selection
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Highly efficient Agrobacterium-mediated transformation of carnation (Dianthus caryophyllus L.) was obtained by first wounding stem explants via microprojectile bombardment. When this was followed by cocultivation with disarmed Agrobacterium in the dark, the transformation frequency-based on transient GUS expression-increased to over 10-fold that of explants wounded by other means and cocultivated under constant light. Two cycles of regeneration/selection on kanamycin were employed to generate stably transformed carnation plants and eliminate chimeras: first, plantlets were regenerated from inoculated stem explants and then leaves from these plantlets were used to generate transgenes in a second selection cycle of adventitious shoot regeneration. Agrobacterium strain AGLO, carrying the binary vector pCGN7001 containing uidA and nptII genes, was used in the stable transformation experiments. The combination of wounding via bombardment, cocultivation in the dark and two cycles of kanamycin selection yielded an overall transformation efficiency of 1–2 transgenes per 10 stem explants for the three carnation varieties analyzed. Histochemical and molecular analyses of marker genes in T0 and T1 generations confirmed the transgenic nature of the selected plants.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-5028
    Keywords: genetic engineering ; 4-hydroxybenzoic acid glucoside ; Lithospermum erythrorhizon ; menisdaurin ; shikonin ; ubiC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The biosynthetic pathway to 4-hydroxybenzoate (4HB), a precursor of the naphthoquinone pigment shikonin, was modified in Lithospermum erythrorhizon hairy root cultures by introduction of the bacterial gene ubiC. This gene of Escherichia coli encodes chorismate pyruvate-lyase (CPL), an enzyme that converts chorismate into 4HB and is not normally present in plants. The ubiC gene was fused to the sequence for a chloroplast transit peptide and placed under control of a constitutive plant promoter. This construct was introduced into L. erythrorhizon by Agrobacterium rhizogenes-mediated transformation. The resulting hairy root cultures showed high CPL activity. 4HB produced by the CPL reaction was utilized for shikonin biosynthesis, as shown by in vivo inhibition of the native pathway to 4HB with 2-aminoindan-2-phosphonic acid (AIP), an inhibitor of phenylalanine ammonia-lyase. A feeding experiment with [1,7-13C2]shikimate showed that in the absence of AIP the artificially introduced CPL reaction contributed ca. 20% of the overall 4HB biosynthesis in the transgenic cultures. ubiC transformation did not lead to a statistically significant increase of shikonin formation, but to a 5-fold increase of the accumulation of menisdaurin, a nitrile glucoside which is presumably related to aromatic amino acid metabolism.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Photosynthesis research 60 (1999), S. 29-42 
    ISSN: 1573-5079
    Keywords: enzyme catalysis ; evolution ; genetic engineering ; photosynthesis ; protein assembly ; protein degradation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco; EC 4.1.1.39) has played a central role in our understanding of chloroplast biogenesis and photosynthesis. In particular, its catalysis of the rate-limiting step of CO2 fixation, and the mutual competition of CO2 and O2 at the active site, makes Rubisco a prime focus for genetically engineering an increase in photosynthetic productivity. Although it remains difficult to manipulate the chloroplast-encoded large subunit and nuclear-encoded small subunit of crop plants, much has been learned about the structure/function relationships of Rubisco by expressing prokaryotic genes in Escherichia coli or by exploiting classical genetics and chloroplast transformation of the green alga Chlamydomonas reinhardtii. However, the complexity of chloroplast Rubisco in land plants cannot be completely addressed with the existing model organisms. Two subunits encoded in different genetic compartments have coevolved in the formation of the Rubisco holoenzyme, but the function of the small subunit remains largely unknown. The subunits are posttranslationally modified, assembled via a complex process, and degraded in regulated ways. There is also a second chloroplast protein, Rubisco activase, that is responsible for removing inhibitory molecules from the large-subunit active site. Many of these complex interactions and processes display species specificity. This means that attempts to engineer or discover a better Rubisco may be futile if one cannot transfer the better enzyme to a compatible host. We must frame the questions that address this problem of chloroplast-Rubisco complexity. We must work harder to find the answers.
    Type of Medium: Electronic Resource
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