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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of fish biology 43 (1993), S. 0 
    ISSN: 1095-8649
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: About 20 ovaries of the whitefish ‘Blaufelchen’ (Coregonus lavaretus L.) of Lake Constance (Bodensee) were collected annually from 1964-1991. Absolute and relative fecundity peaked in the early 1980s, lagging about 2 years behind the maximum of total-P in the water (during the circulation period). Out of the biological time-series of Lake Constance, whitefish fecundity is the only one known to follow the phosphorus curve, and this may be the first time-series documented case of parallel trend reversal in the trophic state of a lake and fish biology. It is concluded that fish fecundity serves, at best, as an unspecific monitor of the overall well-being of the fish.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 50 (1985), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A qualitative screening revealed the occurrence of lipase, esterase, protease, amylase, endo-1,4-β-D-glucanase, xylanase, pectinmethylesterase, polygalacturonase, catalase, β-D-glucosidase and β-D-galactosidase activities in the technical Aspergillus niger enzyme under study (Lipase 2212 D, Röhm). The isolation and purification of lipolytic activities were performed by combination of DEAE-Trisacryl M ion exchange chromatography, Sephadex G 50 gel filtration and hydrophobic chromatography using Phenylsepharose CL-4B. The individual purification steps were checked by specific enzyme visualization in ultrathin agar gels after ultrathin-layer isoelectric focusing (UIEF). Two UIEF homogeneous lipase isoenzymes (I and II) were isolated and characterized by the following parameters: isoelectric points (I: 4.0; II. 3.5); molecular weights (I: 31000 daltons; II: 19000 daltons); carbohydrate contents (I: 6%; II: 9%) and compositions; pH optima (I, II: 5-6); substrate specificities and various effectors.
    Type of Medium: Electronic Resource
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