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  • 1995-1999  (4)
Materialart
Erscheinungszeitraum
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  • 1
    Digitale Medien
    Digitale Medien
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 106 (1997), S. 6385-6389 
    ISSN: 1089-7690
    Quelle: AIP Digital Archive
    Thema: Physik , Chemie und Pharmazie
    Notizen: Pulse radiolysis and emission spectroscopy techniques have been used to examine the production of the 2p1 state of Ar and the 4p 2P1/2 and 4p 2D5/2 states of Ar+ at gas pressures below 1 Torr. The rate of formation of these states has been compared with the results from calculations using the time-dependent Spencer–Fano theory of high-energy electron degradation. It is found that the theory successfully predicts the time scale of events in pulse-irradiated argon gas. © 1997 American Institute of Physics.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 1368-1369 
    ISSN: 1399-0047
    Quelle: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Thema: Chemie und Pharmazie , Geologie und Paläontologie , Physik
    Notizen: 2-Dehydro-3-deoxygalactarate (DDG) aldolase (E.C. 4.1.2.20) catalyzes the reversible aldol cleavage of DDG and 2-dehydro-3-deoxyglucarate to pyruvate and tartronic semialdehyde. Rhombohedral crystals of recombinant DDG aldolase from Escherichia coli K-12 were obtained. The crystals belong to space group R32 with unit-cell parameters a = 93 Å, α = 85°. The crystals diffract to beyond 1.8 Å resolution on a Cu Kα rotating-anode generator. The asymmetric unit is likely to contain two molecules, corresponding to a packing density of 1.34 Å3 Da−1.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 146 (1997), S. 0 
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Klebsiella aerogenes W70 was reported previously to produce a membrane-associated tyramine oxidase (TynA) that did not act on 2-phenylethylamine. Subsequently, a gene cloned from K. aerogenes W70 produced a soluble amine oxidase (MaoA) that acted readily on 2-phenylethylamine and tyramine. This enzyme appeared to be equivalent to a 2-phenylethylamine oxidase of Escherichia coli K-12 (MaoA) but was assumed to be the originally described K. aerogenes W70 tyramine oxidase (TynA). However, as described here, whole cells and cell-free extracts of K. aerogenes W70 showed only the tyramine oxidase (TynA) that is inactive against 2-phenylethylamine and not the maoA gene product. It seems that the organism has two amine oxidase genes, tynA and maoA, but only tynA is expressed. Hence, data relating to the expression of the K. aerogenes W70 tynA gene cannot be assumed to apply to the maoA gene of E. coli K-12 because they encode different enzymes.
    Materialart: Digitale Medien
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  • 4
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 133 (1995), S. 0 
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Abstract Arthrobacter globiformis amine oxidase produced by Escherichia coli cells grown in copper-depleted media was reported to undergo activation due to formation of its topaquinone cofactor in a copper-dependent autocatalytic reaction. Likewise, a mutated E. coli amine oxidase located in the cytoplasm was reported to form topaquinone autocatalytically in an EDTA-sensitive reaction. Here we show unequivocally that formation of an amine oxidase lacking topaquinone is primarily a consequence of the location of the enzyme in the cytoplasm rather than the level of copper in the growth medium. For E. coli, insertion of copper into apoamine oxidase and subsequent topaquinone formation occur after export of the apoenzyme into the periplasm.
    Materialart: Digitale Medien
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