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  • Blackwell Publishing Ltd  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Cyanopeptolin S, a sulfate-containing depsipeptide from a water bloom of Microcystis sp. (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 129 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A new sulfated, cyclic depsipeptide, called cyanopeptolin S, from Microcystis sp. was isolated from a water bloom in the Auensee/Leipzig (Germany). The depsipeptide had a relative molecular mass of 925 and contained l-arginine, l-threonine, l-isoleucine, N-methyl-l-phenylalanine, a l-glutamic acid-δ-aldehyde ring system and a sulfated d-configurated glyceric acid as a side chain. The structure was elucidated by means of two-dimensional 1H and 13C nuclear magnetic resonance spectroscopy, fast atom bombardment mass spectroscopy, Fourier transformed infrared spectroscopy and combined gas-liquid chromatography/mass spectrometry. Cyanopeptolin S inhibited trypsin with an IC50≤ 0.2 μg ml−1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07569.x
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  • 2
    Electronic Resource
    Electronic Resource
    Nitrite reductase activity in Nitrobacter vulgaris (1990)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 67 (1990), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In Nitrobacter vulgaris strain Ab1 a membrane-bound nitrite reductase was found to be co-purified with the nitrite oxidoreductase, the key enzyme system of nitrite oxidizing cells. The relative molecular weight of the enzyme, estimated by SDS-PAGE, was assumed to be 63 000. The pH optimum was shown to be 6.1 and the Km value for nitrite 263 μM. The IEP was calculated to be at pH 5.5–6.0. The enzyme was inhibited by N,N-diethyldithiocarbaminate (DDC), o-phenanthroline and ethylmaliendiimide. Dithionite-reduced benzyl and methyl viologen, NADH/FMN, and dithionite-reduced horse heart cytochrome c were suitable electron donors for nitrite reduction. The enriched enzyme produced NO as the only end product and showed weak cytochrome c oxidase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1990.tb13847.x
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    Paper (German National Licenses)
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