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  • Chemistry  (2)
  • Nutrients
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  • 1
    Electronic Resource
    Electronic Resource
    The species composition of Antarctic phytoplankton interpreted in terms of Tilman's competition theory (1988)
    Springer
    Oecologia 77 (1988), S. 464-467 
    Details
    ISSN: 1432-1939
    Keywords: Antarctic phytoplankton ; Competition ; Resource ratios ; Nutrients
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary An attempt was made, to test for the impact of resource competition on Antarctic marine phytoplankton. According to theory, species composition near competitive equilibrium should be determined by the ratios of limiting resources. Enrichment bioassays identified silicon and nitrogen as limiting nutrients for some of the most important phytoplankton species during early austral summer in the region near the Antarctic Peninsula. Together with the generally acknowledged limiting resource light, this gave three meaningful ratios of essential resources (Si:N, Si:light, N:light) and one ratio of substitutable resources (NO3:NH4). Phytoplankton species assemblages were found to be well separated by the ratios of the essential resources and by mixing depth. Nine out of 12 individual species were found to be separated along at least one of the gradients of resource ratios. Where comparison with competition experiments was available, predicted and realized distributions of species were compatible.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00377261
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  • 2
    Electronic Resource
    Electronic Resource
    Physical properties of β-N-acetyl-D-glucosaminidase and β-N-acetyl-D-hexosaminidase from Drosophila Kc-cells (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 18 (1991), S. 45-53 
    Details
    ISSN: 0739-4462
    Keywords: molecular mass ; pH and temperature optima ; thermal stability ; influence of ionic strength ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Kc-cells from Drosophila produce two different β-D-hexosaminidases, a β-N-acetyl-D-glucosaminidase (E.C.3.2.1.30) and a β-N-acetyl-D-hexosaminidase (E.C.3.2.1.52), which are also secreted into the medium. The Mr of both enzymes is about 126,000 ± 9,700; the S-values are 8.37 ± 0.44. Both enzymes have about the same pH optima at 5.5 and the same thermal stability. The temperature optima are identical (50°C) for both enzymes if p-nitrophenyl-N-acetylglucosaminide is used as a substrate. However, when p-nitrophenyl-N-acetylgalactoseaminide is used as the substrate the β-N-acetyl-D-hexosaminidase has a temperature optimum about 10°C higher. With higher salt concentrations, the activity of the β-N-acetyl-D-glucosaminidase increases, whereas β-N-acetyl-D-hexosaminidase is inhibited. Both enzymes also differ in their sensitivity to urea, the β-N-acetyl-D-hexosaminidase being less sensitive than the β-N-acetyl-D-glucosaminidase.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940180105
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  • 3
    Electronic Resource
    Electronic Resource
    Demonstration of β-N-acetyl-D-glucosaminidase and β-N-acetyl-D-hexosaminidase in Drosophila Kc-cells (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 17 (1991), S. 3-13 
    Details
    ISSN: 0739-4462
    Keywords: intra- and extracellular enzymes ; kinetic properties ; inhibition ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Kc-cells from Drosophila melanogaster, grown under serum-free conditions, produce two β-hexosaminidases and secrete these enzymes into the medium. The two enzymes were separated by DEAE-exchange chromatography. According to their substrate specificities one enzyme is a β-N-acetyl-D-glucosaminidase (E.C.3.2.1.30), the other one a β-N-acetyl-D-hexosaminidase (E.C.3.2.1.52). The β-N-acetyl-D-glucosaminidase is predominant in the medium, the β-N-acetyl-D-hexosaminidase within the cells. The Km values for the substrates pNP-GlcNAc, pNP-GalNAc, and (GlcNAc)2 are 0.8, 16.73, and 1.67 mM for the β-N-acetyl-D-glucosaminidase and 0.24, 0.44, and 0.2 mM for the β-N-acetyl-D-hexosaminidase. Both enzymes are inhibited by the products and the β-N-acetyl-D-glucosaminidase is also inhibited stereospecifically by the substrates pNP-GlcNAc and (GlcNAc)2. Both enzymes are inhibited in a partial competitive way by acetamidolactones, the Kis being as low as 0.1 μM.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940170103
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