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  • 1
    Electronic Resource
    Electronic Resource
    Formation of red pigment during wood decay caused by white-rot fungi (1966)
    Springer
    Cellular and molecular life sciences 22 (1966), S. 517-518 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Zusammenfassung Holzzerstörende Pilze, die ins Medium Polyphenolasen ausscheiden, bilden bei der Zersetzung des Holzes, welches mit 3% Peptonlösung aufgesogen wurde, ein rotes Pigment. Die Pigmentbildung ist durch die sekundäre Oxydation von Aminosäuren und die katalysierende Rolle der Polyphenolasen verursacht.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01898663
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Function of enzymes in wood decaying fungi (1971)
    Springer
    Archives of microbiology 77 (1971), S. 140-150 
    Details
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. Mycelial extracts and culture filtrates of two species of Trametes have been assayed for various enzymatic activities. The tests performed after 3 and 10 days of mycelial growth on 3% malt extract have revealed that the spectra of external enzymes secreted by both strains differ markedly from their intracellular equivalents. A great part of the external isozyme bands, shown in disc electrophoresis and isoelectric focusing, have no equivalent acting within the cell. 2. These findings are discussed on the basis of special functional properties which have to be attributed to external enzymes. It is concluded that a great number of them are not simply internal enzymes which happen to be active outside the cell but that they are synthesized or at least modified especially for extracellular action under these special conditions. 3. A comparison between the two species of Trametes has shown that both produce enzymes with identical function. This indicates their strong relationship, though the electrophoretic mobility of most of the enzymes is not comparable. The consequences of these findings for chemical taxonomy are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00408606
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Purification and Characterization of Glutamine Synthetase from the Basidiomycete Pleurotus ostreatus (1996)
    Springer
    Current microbiology 33 (1996), S. 181-186 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The purification and some properties of glutamine synthetase (GS) from the mycelium of the basidiomycete Pleurotus ostreatus are described. The enzyme was purified to apparent homogeneity with ion exchange chromatography and a Dyematrex Green A column as the major purification steps. The GS has a molecular weight of 470 kDa and is composed of eight subunits with a molecular weight of 58 kDa. A tetrameric form of the enzyme may also be active. The apparent K m values for the biosynthetic reaction varied in different mycelial extracts from 2.5 to 3.5 mM and from 0.02 to 0.06 for glutamate and ammonium respectively. In the transferase reaction, K m values of 48 mM and 6.2 mM were found for L-glutamine and hydroxylamine, respectively. From the divalent cations tested, Mn2+ showed the strongest stimulatory effect both on the transferase and the biosynthetic reaction. ADP was the only nucleotide having an activating effect on the transferase reaction. The biosynthetic reaction was strongly inhibited by AMP and the transferase reaction by carbamoylphosphate. L-Alanine and glycine inhibited both reactions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002849900097
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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