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  • 1
    Electronic Resource
    Electronic Resource
    Molecular characterization of the glnA gene encoding glutamine synthetase from the edible mushroom Agaricus bisporus (1997)
    Springer
    Molecular genetics and genomics 256 (1997), S. 179-186 
    Details
    ISSN: 1617-4623
    Keywords: Key wordsAgaricus bisporus ; Glutamine synthetase ; Molecular cloning ; Gene structure ; Mushroom
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The gene encoding glutamine synthetase (glnA) was isolated from an Agaricus bisporus H39 recombinant λ phage library. The deduced A. bisporus glutamine synthetase amino acid sequence contains 354 residues. The amino acid sequence is very similar to that derived from the gene coding for glutamine synthetase of the yeast Saccharomyces cerevisiae. The open reading frame is interrupted by four introns. Northern analysis revealed that transcription of the gene is repressed upon addition of ammonium to the culture but the repression was not as strong as that of the gene encoding NADP+-dependent glutamate dehydrogenase (gdhA). Enzyme activities are low in the presence of ammonium, glutamine and albumin and do not correlate with the mRNA levels revealed by Northern analysis. This suggests that glutamine synthetase expression in A. bisporus is also post-transcriptionally regulated by the nitrogen source.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00008612
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  • 2
    Electronic Resource
    Electronic Resource
    NAD+-dependent glutamate dehydrogenase of the edible mushroom Agaricus bisporus: biochemical and molecular characterization (1999)
    Springer
    Molecular genetics and genomics 261 (1999), S. 452-462 
    Details
    ISSN: 1617-4623
    Keywords: Key wordsAgarcius bisporus ; NAD+-specific glutamate dehydrogenase ; Molecular cloning ; Gene structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The NAD+-dependent glutamate dehydrogenase (NAD-GDH) of Agaricus bisporus, a key enzyme in nitrogen metabolism, was purified to homogeneity. The apparent molecular mass of the native enzyme is 474 kDa comprising four subunits of 116 kDa. The isoelectric point of the enzyme is about 7.0. K m values for ammonium, 2-oxoglutarate, NADH, glutamate and NAD+ were 6.5, 3.5, 0.06, 37.1 and 0.046 mM, respectively. The enzyme is specific for NAD(H). The gene encoding this enzyme (gdhB) was isolated from an A. bisporus H39 recombinant λ phage library. The deduced amino acid sequence specifies a 1029-amino acid protein with a deduced molecular mass of 115,463 Da, which displays a significant degree of similarity with NAD-GDH of Saccharomyces cerevisiae and Neurospora crassa. The ORF is interrupted by fifteen introns. Northern analysis combined with enzyme activity measurements suggest that NAD-GDH from A. bisporus is regulated by the nitrogen source. NAD-GDH levels in mycelium grown on glutamate were higher than NAD-GDH levels in mycelium grown on ammonium as a nitrogen source. Combined with the kinetic parameters, these results suggest a catabolic role for NAD-GDH. However, upon addition of ammonium to the culture transcription of the gene is not repressed as strongly as that of the gene encoding NADP-GDH (gdhA). To date, tetrameric NAD-GDHs with large subunits, and their corresponding genes, have only been isolated from a few species. This enzyme represents the first NAD-GDH of basidiomycete origin to be purified and is the first such enzyme from basidiomycetes whose sequence has been determined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050988
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  • 3
    Electronic Resource
    Electronic Resource
    A new erythroid cell line induced by Rauscher murine leukaemia virus (1978)
    [s.l.] : Nature Publishing Group
    Nature 272 (1978), S. 626-628 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The tumours were induced by subcutaneous transplantation of liver fragments and could be transplanted serially both in solid and in ascites form. (DBAXC57B1) and (DB Ax BALB/c) Fi crosses were also successful hosts for tumour transplantation, whereas transplantation failed in BALB/c mice. The ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/272626a0
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  • 4
    Electronic Resource
    Electronic Resource
    Substrate dependent larval development and emergence of the mushroom pests Lycoriella auripila and Megaselia halterata (1996)
    Springer
    Entomologia experimentalis et applicata 79 (1996), S. 329-334 
    Details
    ISSN: 1570-7458
    Keywords: sciarids ; phorids ; mushroom compost ; casing soil ; Agaricus bisporus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Pasteurized, spawned, full-grown and immediately-cased full-grown compost were simultaneously exposed to natural populations of the mushroom pests Lycoriella auripila (Winnertz) (Diptera: Sciaridae) and Megaselia halterata (Wood) (Diptera: Phoridae). Different numbers of adults emerged from each of these composts. Highest numbers of L. auripila emerged from spawned and pasteurized compost whereas lowest numbers of L. auripila emerged from full-grown compost. the emergence from full-grown compost was delayed, which could be explained by the delayed development of the larvae in this type of compost. High numbers of M. halterata emerged from compost that was completely colonized by the mycelia of the edible white button mushroom Agaricus bisporus (Lange) Imbach. The immediate covering of the compost with a casing layer significantly lowered the numbers of emerging M. halterata flies. Compared with the emergence pattern from full-grown and immediately-cased full-grown compost, adult M. halterata showed a delayed pattern of emergence in spawned compost. Adult M. halterata did not emerge from pasteurized compost. The results of these experiments enabled us to improve the timing of the application of insect pathogenic nematodes in the control of the larvae of both insect pests.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00186291
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  • 5
    Electronic Resource
    Electronic Resource
    Location of immature stages of the mushroom insect pest Megaselia halterata in mushroom-growing medium (1997)
    Springer
    Entomologia experimentalis et applicata 83 (1997), S. 323-327 
    Details
    ISSN: 1570-7458
    Keywords: Agaricus bisporus ; sciarid flies ; Lycoriella auripila ; phorid flies ; Megaselia halterata ; biological control ; insect pathogenic nematodes ; Steinernema feltiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Experiments were conducted to examine the location of oviposition by the phorid fly Megaselia halterata (Wood) (Diptera: Phoridae) in uncased and cased compost. Clearly, a majority of the gravid females choose oviposition sites directly after entering the top layer of the compost. In uncased compost, 60% of all adults emerged from the top of four compost layers of equal thickness. When the compost was covered by a casing layer which was still uncolonized by Agaricus bisporus, oviposition was further concentrated in the top compost layer. In this situation, 91% of all adults emerged from the top compost layer whereas only 1.5% emerged from the casing. When the casing layer was colonized by mushroom mycelium, 45% of all adults emerged from the casing layer and 53% emerged from the top compost layer. Further concentration in the top compost layer and the casing layer occurred as a result of upward migration of larvae. When compost was cased after oviposition, up to 43% of all adults emerged from the casing layer. We concluded that in the control of phorid infestations with insect pathogenic nematodes, applications in uncased compost can be restricted to the upper compost layer. When compost and casing are filled simultaneously, nematode applications in the casing layer only could be considered.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1002998916843
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  • 6
    Electronic Resource
    Electronic Resource
    Mushroom worker's lung: Serologic reactions to thermophilic actinomycetes present in the air of compost tunnels (1993)
    Springer
    Mycopathologia 122 (1993), S. 21-28 
    Details
    ISSN: 1573-0832
    Keywords: Actinomycetes ; Allergy ; Compost ; ELISA ; Lung disease ; Mushroom
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Vast numbers of spores of the thermophilic actinomycetesExcellospora flexuosa,Thermomonospora alba,T. curvata andT. fusca were collected from the air in fermentation tunnels during the spawning of mushroom compost, i.e. over 109 CFU m−3 of air. Five different genera of fungi, namely,Aspergillus,Aureobasidium,Cladosporium,Penicillium andScytalidium, were found at only 103 CFU m−3 of air.Agaricus bisporus, used for spawning, was absent. Sera of 10 mushroom growers affected by Mushroom Worker's Lung (MWL) were tested by a qualitative dot-ELISA for antibodies against the spores of these micro-organisms. All 10 were positive for one or more of the actinomycetesE. flexuosa,T. alba,T. curvata andT. fusca. No antibodies were found againstStreptomyces thermovulgaris,Thermoactinomyces vulgaris andT. sacchari nor against the fungiAspergillus fumigatus,Penicillium brevicompactum,P. chrysogenum,Scytalidium thermophilum andTrichoderma viride. Sera of 11 of 14 workers engaged in routine spawning of compost in tunnels reacted positively with 1 or more of the actinomycetes. Their10log serum titres increased with the duration of employment to an upper limit of 2.5. The sera of 19 non-exposed individuals were negative. Because high numbers of spores ofE. flexuosa,T. alba,T. curvata andT. fusca were present in the air that was used for successful inhalation provocation of mushroom workers with MWL and because of the elevated serum titres of these workers, we presume these organisms to contribute in the occurrence of MWL.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01103705
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  • 7
    Electronic Resource
    Electronic Resource
    Nucleotide sequence and expression of the gene encoding NADP+-dependent glutamate dehydrogenase (gdhA) fromAgaricus bisporus (1996)
    Springer
    Molecular genetics and genomics 250 (1996), S. 339-347 
    Details
    ISSN: 1617-4623
    Keywords: Agaricus bisporus ; NADP+-dependent glutamate dehydrogenase ; Molecular cloning ; Gene structure ; Mushroom
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The gene encoding NADP+-dependent glutamate dehydrogenase (gdhA) was isolated from anAgaricus bisporus recombinant phageλ library. The deduced amino acid sequence would specify a 457-amino acid protein that is highly homologous in sequence to those derived from previously isolated and characterized genes coding for microbial NADP+-GDH. The open reading frame is interrupted by six introns. None of the introns is located at either one of the positions of the two introns conserved in the corresponding open reading frames of the ascomycete fungiAspergillus nidulans andNeurospora crassa. Northern analysis suggests that theA. bisporus gdhA gene is transcriptionally regulated and that, unlike the case in ascomycetes, transcription of this gene is repressed upon the addition of ammonium to the culture.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02174392
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  • 8
    Electronic Resource
    Electronic Resource
    Nucleotide sequence and expression of the gene encoding NADP+-dependent glutamate dehydrogenase (gdhA) from Agaricus bisporus (1996)
    Springer
    Molecular genetics and genomics 250 (1996), S. 339-347 
    Details
    ISSN: 1617-4623
    Keywords: Key words Agaricus bisporus ; NADP+-dependent glutamate dehydrogenase ; Molecular cloning ; Gene structure ; Mushroom
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  The gene encoding NADP+-dependent glutamate dehydrogenase (gdhA) was isolated from an Agaricus bisporus recombinant phage λ library. The deduced amino acid sequence would specify a 457-amino acid protein that is highly homologous in sequence to those derived from previously isolated and characterized genes coding for microbial NADP+-GDH. The open reading frame is interrupted by six introns. None of the introns is located at either one of the positions of the two introns conserved in the corresponding open reading frames of the ascomycete fungi Aspergillus nidulans and Neurospora crassa. Northern analysis suggests that the A. bisporus gdhA gene is transcriptionally regulated and that, unlike the case in ascomycetes, transcription of this gene is repressed upon the addition of ammonium to the culture.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02174392
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  • 9
    Electronic Resource
    Electronic Resource
    Purification and characterization of NADP-dependent glutamate dehydrogenase from the commercial mushroom Agaricus bisporus (1995)
    Springer
    Current microbiology 30 (1995), S. 211-217 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The nicotinamide adenine dinucleotide phosphate (NADP)-dependent glutamate dehydrogenase (NADP-GDH) of Agaricus bisporus, a key enzyme in ammonia assimilation, was purified to apparent electrophoretic homogeneity with 27% recovery of the initial activity. The molecular weight of the native enzyme was 330 kDa. The enzyme is probably a hexamer, composed of identical subunits of 48 kDa. The isoelectric point of the enzyme was found at pH 4.8. The N-terminus appeared to be blocked. The enzyme was specific for NADP(H). The Km-values were 2.1, 3.2, 0.074, 27.0, and 0.117mM for ammonia, 2-oxoglutarate, NADPH, L-glutamate, and NADP respectively. The pH optima for the amination and deamination reactions were found to be 7.6 and 9.0, respectively. The temperature optimum was 33°C. The effect of several metabolites on the enzyme's activity was tested. Pyruvate, oxaloacetate, ADP, and ATP showed some inhibitory effect. Divalent cations slightly stimulated the aminating reaction. Antibodies raised against the purified enzyme were able to precipitate NADP-GDH activity from a cell-free extract in an anticatalytic immunoprecipitation test. Analysis of a Western blot showed the antibodies to be specific for NADP-GDH.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00293635
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  • 10
    Electronic Resource
    Electronic Resource
    Purification and characterization of glutamine synthetase from the commerical mushroom Agaricus bisporus (1995)
    Springer
    Current microbiology 31 (1995), S. 108-113 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Agaricus bisporus glutamine synthetase, a key enzyme in nitrogen metabolism, was purified to apparent homogeneity. The native enzyme appeared to be a GS-II type enzyme. It has a molecular weight of 325 kDa and consists of eight 46-kDa subunits. Its pI was found at 4.9. Optimal activity was found at 30°C. The enzyme had low thermostability. Stability declined rapidly at temperatures above 20°C. The enzyme exhibits a K m for glutamate, ammonium, and ATP of 22mm, 0.16mm and 1.25mm respectively in the biosynthetic reaction, with optimal activity at pH 7. The enzyme is slightly inhibited by 10mm concentrations of l-alanine, l-histidine, l-tryptophan, anthranilic acid, and 5′-AMP and was strongly inhibited by methionine sulfoximine and phosphinothricine. For the transferase reaction K i-values were 890 μm and 240 μm for methionine sulfoximine and phosphinothricine respectively. For the biosynthetic reaction K i was 17 μm for both methionine sulfoximine and phosphinothricine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00294285
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