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  • 1
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 4 (1989), S. 484-499 
    ISSN: 0884-3996
    Keywords: Luminescence ; chromatography ; detection ; quantitative analysis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: An overview is presented of the physicochemical basis of luminescence, and its application to the detection of chemicals (drugs, biomedically important compounds, environmentally active substances) in liquid chromatographic systems.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 6 (1987), S. 97-107 
    ISSN: 0739-4462
    Keywords: hybridoma ; ELISA ; immunoblotting ; apolipoproteins ; locust ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Spleen lymphocytes from mice immunized with locust native low-density lipophorin A+ (LDLp) were fused with nonproducing myeloma cells, strain Sp 2/0. Hybridomas that were isolated from the fused cells produced antibodies specific for LDLp and the high-density lipophorin Ayellow (HDLp).Monoclonal strains were generated through cloning by limiting dilution from those hybridomas synthesizing antibodies specific for apolipophorins (apoLp)-I, -II, and -III of LDLp. Additionally, a hybridoma strain that was obtained after fusion of lymphocytes from mice immunized with apoLp-III produced antibodies that bind to apoLp-III and native LDLp.Some features of LDLp and HDLp were studied using these antibodies. It could be demonstrated that apoLp-I and apoLp-II are not immunochemically identical and are exposed in the native particle of both LDLp and HDLp. It was also shown that in both lipophorins apoLp-II is less exposed than apoLp-I, whereas in LDLp apoLp-III is mainly exposed; some apoLp-III could also be detected in HDLp.Tween-20, a nonionic detergent, appears to affect the binding of anti-apoLp-I, -II, and -III to both LDLp and HDLp. The monoclonal antibodies specific for locust apolipophorins do not bind to the respective apoproteins of lipophorins from other insects.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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