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  • 1
    Electronic Resource
    Electronic Resource
    Isolation, Purification, and Characterization of Lipase Isoenzymes from a Technical Aspergillus niger Enzyme (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 50 (1985), S. 0 
    Details
    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
    URL: http://dx.doi.org/10.1111/j.1365-2621.1985.tb10574.x
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  • 2
    Electronic Resource
    Electronic Resource
    Fecundity of whitefish (Coregonus lavaretus) during the eu-and oligotrophication of Lake Constance (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of fish biology 43 (1993), S. 0 
    Details
    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
    URL: http://dx.doi.org/10.1111/j.1095-8649.1993.tb00412.x
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  • 3
    Electronic Resource
    Electronic Resource
    Crustal structure of the Lofoten continental margin, off northern Norway, from ocean-bottom seismographic studies (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Geophysical journal international 121 (1995), S. 0 
    Details
    ISSN: 1365-246X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Geosciences
    Notes: In 1988, an extensive geophysical experiment was performed on the Lofoten passive continental margin, which was formed by the continental break-up between Greenland and northern Norway at 58 Ma. The geological units of the outer Lofoten margin are characterized by seaward-dipping reflectors (SDRs) and landward flood basalt, which extends up to 100 km landwards of SDRs. In this study, we obtain the P-wave velocity structure beneath the Lofoten Basin, the SDRs, and the landward flood basalt by use of ocean-bottom seismograph refraction profiling, and we also discuss the formation of the northern Norwegian passive continental margin.In the Lofoten Basin the crust is of oceanic type, consisting of sedimentary layers, oceanic laver 2 (4.9−5.5 km s−1), layer 3A (6.3−6.8 km s−1) and layer 3B (7.0−7.1 km s−1). Beneath the SDRs the crustal layers are identical to those of the Lofoten Basin, but the thickness of the lower crust, which represents the same velocity as layer 3B, increases to 5 km towards the continent side, and a high-velocity lower crustal layer (7.3 km s−1) is formed at the base of the crust. The ocean-continent transition zone is situated between the landward side of the SDRs and the northward continuation of the Vøring Plateau Escarpment. In this region the velocity of the lower crust gradually decreases and approaches the lower crustal velocity beneath the Lofoten Islands (6.8 km s−1). The model also indicates that the high-velocity layer disappears in this region. Comparing our model with the crustal structure on the Vøring margin, it is clear that the lower crustal body (≥7 km s−1) thickens southwards along the northern Norwegian continental margin. Recent results from petrological and geophysical studies of the generation of the oceanic crust have shown that increasing the temperature of the upwelling asthenospheric material increases the thickness of the oceanic crust. We interpret this as that the oceanic crust in the southern area in the Vøring-Lofoten margin was generated by hotter material than that of the northern area.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-246X.1995.tb06447.x
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  • 4
    Electronic Resource
    Electronic Resource
    Distribution of parvalbumin isotypes in adult snook and their potential applications as species-specific biomarkers (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of fish biology 51 (1997), S. 0 
    Details
    ISSN: 1095-8649
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The highly stable Ca2+ binding protein, parvalbumin, is prevalent in fish white muscle tissue. The properties of this protein make it a promising antigen for use as a specific biomarker for fish identification. Parvalbumin was purified from white muscle of an adult common snook Centropomus undecimalis using ammonium sulfate precipitation, size-exclusion chromatography (SEC) and anion-exchange HPLC. Parvalbumins were characterized by the presence of an 11-kDa band following gradient-SDS gel electrophoresis and by their immunoreactivity against mouse anti-parvalbumin antibodies. Anion-exchange chromatography of the parvalbumin fraction separated from the SEC column yielded nine fractions. Subsequent analysis of these fractions by isoelectric focusing gel electrophoresis led to a total of seven parvalbumin isotypes, which may lend themselves as biomarkers in fish identification. The presence of these seven parvalbumin isotypes was confirmed independently by reversed-phase HPLC. A dilution endpoint immunoassay was developed for C. undecimalis parvalbumin using a monoclonal antibody directed against its highly conserved calcium binding site. The utility of parvalbumin isotype distribution and specific monoclonal antibodies against fish parvalbumin in species identification is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1095-8649.1997.tb01512.x
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