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  • Electronic Resource  (7)
  • 1995-1999  (4)
  • 1980-1984  (3)
  • Recombinant DNA
  • 1
    Electronic Resource
    Electronic Resource
    Strategies for gene cloning (1999)
    Springer
    Urological research 27 (1999), S. 83-96 
    Details
    ISSN: 1434-0879
    Keywords: Key words Genitourinary malignancies ; Recombinant DNA ; Gene cloning ; DNA chip technology ; Diagnostics ; Gene therapy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Cancer, including genitourinary malignancy, is a consequence of accumulated genetic aberrations in genes involved in crucial regulatory pathways. The result is a deregulation of cellular behaviour, leading to neoplastic transformation, uncontrolled cell proliferation and acquisition of metastatic ability. The development and perfection of techniques in the field of recombinant DNA technology, gene cloning, (differential) analysis of gene expression, and sequencing of genes and proteins have provided a wealth of information about the genetic aberrations associated with cancer development. This “recombinant DNA and gene cloning” technology and the recently developed DNA chip technology may provide new molecular diagnostic tools. Furthermore, the technology of gene cloning in combination with the progress in in vivo gene delivery techniques offers new treatment modalities, like gene therapy, additional to conventional therapies. This review is intended to provide a general introduction to the fundamentals or strategies of recombinant DNA and gene cloning techniques as a basis for understanding the rapidly expanding range of new diagnostic and therapeutic opportunities. Some illustrative examples are provided, addressing basic and biomedical research and possible clinical applications in genitourinary oncology.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002400050093
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  • 2
    Electronic Resource
    Electronic Resource
    Cloning and expression of the Apa LI, Nsp I, Nsp HI, Sac I, Sca I, and Sap I restriction-modification systems in Escherichia coli (1998)
    Springer
    Molecular genetics and genomics 260 (1998), S. 226-231 
    Details
    ISSN: 1617-4623
    Keywords: Key words Restriction endonuclease ; Methylase selection ; Gene expression ; DNA methylation ; Recombinant DNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The genes encoding the ApaLI (5′-G^TGCAC-3′), NspI (5′-RCATG^Y-3′), NspHI (5′-RCATG^Y-3′), SacI (5′-GAGCT^C-3′), SapI (5′-GCTCTTCN1^-3′, 5′-^N4GAAGAGC-3′) and ScaI (5′-AGT^ACT-3′) restriction-modification systems have been cloned in E.␣coli. Amino acid sequence comparison of M.ApaLI, M.NspI, M.NspHI, and M.SacI with known methylases indicated that they contain the ten conserved motifs characteristic of C5 cytosine methylases. NspI and NspHI restriction-modification systems are highly homologous in amino acid sequence. The C-termini of the NspI and NlaIII (5′-CATG-3′) restriction endonucleases share significant similarity. 5mC modification of the internal C in a SacI site renders it resistant to SacI digestion. External 5mC modification of a SacI site has no effect on SacI digestion. N4mC modification of the second base in the sequence 5′-GCTCTTC-3′ blocks SapI digestion. N4mC modification of the other cytosines in the SapI site does not affect SapI digestion. N4mC modification of ScaI site blocks ScaI digetion. A DNA invertase homolog was found adjacent to the ApaLI restriction-modification system. A DNA transposase subunit homolog was found upstream of the SapI restriction endonuclease gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050890
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Norms for patents concerning human and other life forms (1996)
    Springer
    Theoretical medicine and bioethics 17 (1996), S. 279-314 
    Details
    ISSN: 1573-1200
    Keywords: Recombinant DNA ; transgenesis ; patents ; human life forms
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine , Philosophy
    Notes: Abstract The rationale of patents on transgenic organisms leads to the startling notion of the human qua infringement. The moral reasons by which we may tenably reject such notion are not conclusive as to human life forms outside the body. A close look at recombinant DNA experimentation reveals ingenious processes, but not entities that the body lacks. Except for artificial genes, the genes of biotechnology are found on chromosomes, albeit nonconsecutively, and their uninterrupted transcripts appear in messenger RNA. An enhanced form of protection for ingenious processes, the “human methods patent,” is proposed and defended as a replacement for product patents. The proposed patent would pertain to biotechnology manufacturing and genetic intervention in somatic and germ cells. A counterpart could govern nonhuman life forms. It is argued that compulsory licensing protections should be a condition of such patent. Contrary to the conservative assumption that statutory sobriquets suffice, the reckoning of what qualifies as a patentable ingenious process will continue to require systematic scientific guidance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00489450
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    A novel strategy for the isolation of defined pyrG mutants and the development of a site-specific integration system for Aspergillus awamori (1995)
    Springer
    Current genetics 27 (1995), S. 536-540 
    Details
    ISSN: 1432-0983
    Keywords: Recombinant DNA ; Filamentous fungi ; 5-fluoro-orotic acid ; Homologous transformation system
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A homologous gene transfer system for Aspergillus awamori for site-specific integration is described, based on two components. First, a defined A. awamori pyrG mutant strain constructed by a selection strategy for gene-replacement in fungi. Second, a vector with a homologous pyrG selection marker containing a defined mutation at a site different from that of the mutations in the pyrG gene of the defined mutant strain. Defined mutation in the A. awamori pyrG gene, isolated from a genomic library by heterologous hybridisation with the A. niger pyrG gene as a probe, were introduced by specifically altering sequences at restriction sites in the coding region of the gene. After transformation of the A. awamori wild-type strain with vectors containing these mutated pyrG genes, and selection for 5-fluoro-orotic acid resistance (5-FOAR), on the average 60% of the 5-FOAR colonies originated from replacement of the wild-type pyrG gene by the mutated pyrG allele. After transformation of a mutant strain, carrying a mutation near the 5′ end of the pyrG gene with vectors containing a mutation near the 3′ end of the pyrG gene, 35% of the resulting transformants contained one copy of the vector at the pyrG locus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00314444
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  • 5
    Electronic Resource
    Electronic Resource
    Cloning of the ribokinase gene of Staphylococcus hyicus subsp. hyicus in Staphylococcus carnosus (1984)
    Springer
    Archives of microbiology 140 (1984), S. 218-224 
    Details
    ISSN: 1432-072X
    Keywords: Recombinant DNA ; Cloning ; Staphylococcus carnosus and S. hyicus subsp. hyicus ; Ribose degradation ; Ribokinase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A gene library with DNA of Staphylococcus hyicus subsp. hyicus was established in S. carnosus by using the plasmid vector pCT20. Two clones of S. carnosus were isolated which were able to ferment d-ribose. The two hybrid plasmids (pRib 1) and (pRib 2) were isolated and characterized. They contained inserted DNA fragments of S. hyicus subsp. hyicus with sizes of 10.2 and 8.2 kb, respectively. d-Ribose uptake and enzyme activities were studied. All strains tested [S. hyicus subsp. hyicus, S. carnosus (wild type) and the two S. carnosus clones] possessed an inducible uptake system for d-ribose. S. hyicus subsp. hyicus possessed in addition enzyme activities of d-ribokinase and d-ribose-5-P isomerase. None of these enzyme activities could be detected in S. carnosus (wildtype). Only in the S. carnosus clones containing (pRib 1) or (pRib 2) could a d-ribokinase activity be demonstrated, indicating that the gene for d-ribokinase of S. hyicus subsp. hyicus was cloned in S. carnosus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00454931
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  • 6
    Electronic Resource
    Electronic Resource
    Cloning and analysis of recombinant plasmids containing genes for Aspergillus nidulans 5 S rRNA (1981)
    Springer
    Current genetics 4 (1981), S. 173-176 
    Details
    ISSN: 1432-0983
    Keywords: Aspergillus ; 5S rRNA ; Recombinant DNA ; Restriction Analysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Genes coding for 5S rRNA were found to be dispersed in the Aspergillus nidulans genome. Three different recombinant plasmids hybridizing to 5S rRNA were isolated and their restriction enzyme maps were established.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00420494
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  • 7
    Electronic Resource
    Electronic Resource
    Cloned ß-galactosidase gene of Escherichia coli is expressed in the yeast Saccharomyces cerevisiae (1980)
    Springer
    Current genetics 2 (1980), S. 109-113 
    Details
    ISSN: 1432-0983
    Keywords: Recombinant DNA ; 2 µm DNA ; Heterologous gene expression ; Eukaryotic host
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The expression of the lacZ gene of E. coli in S. cerevisiae has been studied. The enzymatic activity coded by the lacZ gene in E. coli, β-galactosidase, is detectable in yeast cells harboring a chimeric plasmid carrying the gene. On the basis of size and immunological criteria, no difference was detected between the Coli-in-yeast β-galactosidase and the E. coli enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00420622
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    Paper (German National Licenses)
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