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  • 1
    ISSN: 1432-0983
    Keywords: Laccas ; Phenol-oxidas ; Rhizoctonia solani ; Fungi
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Four distinct laccase genes,lcc1, lcc2, lcc3 andlcc4, have been identified in the fungusRhizoctonia solani. Both cDNA and genomic copies of these genes were isolated and characterized. Hybridization analyses indicate that each of the four laccase genes is present in a single copy in the genome. TheR. solani laccases can be divided into two groups based on their protein size, intron/exon organization, and transcriptional regulation. Three of these enzymes have been expressed in the fungusAspergillus oryzae. Two of the recombinant laccases, r-lccl and r-lcc4, as well as the native lcc4 enzyme were purified and characterized. The purified proteins are homodimeric, comprised of two subunits of approximately 66 kDa for lcc4 and 50–100 kDa for the recombinant lccl protein. These laccases have spectral properties that are consistent with other blue copper proteins. With syringaldazine as a substrate, lcc4 has optimal activity at pH 7, whereas lcc1 has optimal activity at pH 6.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0983
    Keywords: Key words Laccas ; Phenol-oxidas ; Rhizoctonia solani ; Fungi
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Four distinct laccase genes, lcc1, lcc2, lcc3 and lcc4, have been identified in the fungus Rhizoctonia solani. Both cDNA and genomic copies of these genes were isolated and characterized. Hybridization analyses indicate that each of the four laccase genes is present in a single copy in the genome. The R. solani laccases can be divided into two groups based on their protein size, intron/exon organization, and transcriptional regulation. Three of these enzymes have been expressed in the fungus Aspergillus oryzae. Two of the recombinant laccases, r-lcc1 and r-lcc4, as well as the native lcc4 enzyme were purified and characterized. The purified proteins are homodimeric, comprised of two subunits of approximately 66 kDa for lcc4 and 50–100 kDa for the recombinant lcc1 protein. These laccases have spectral properties that are consistent with other blue copper proteins. With syringaldazine as a substrate, lcc4 has optimal activity at pH 7, whereas lcc1 has optimal activity at pH 6.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Review of industrial organization 8 (1993), S. 419-433 
    ISSN: 1573-7160
    Keywords: Airline pricing ; deregulation ; contestability ; hub-and-spoke system
    Source: Springer Online Journal Archives 1860-2000
    Topics: Economics
    Notes: Abstract This paper examines airline pricing and market structure determination for domestic airport-pair routes. The model includes variables to control for the effects of congestion, consumer brand preferences, barriers to entry into airports, and multiple airport availability within a city. The results indicate the noncontestability of airline markets, but certain factors can mitigate a carrier's endpoint dominance. Additionally, the need for policies addressing airport congestion is indicated by several aspects of model results.
    Type of Medium: Electronic Resource
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