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  • 1
    Electronic Resource
    Electronic Resource
    Chemiluminescent immunoassay (CLIA) for salmon growth hormone (GH) (1997)
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 12 (1997), S. 271-275 
    Details
    ISSN: 0884-3996
    Keywords: chemiluminescent immunoassay ; acridinium ester ; fish ; salmon ; growth hormone ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A highly sensitive and specific chemiluminescent immunoassay (CLIA) was developed for quantification of growth hormone (GH) in salmonid species. The CLIA for salmon GH was performed using the sandwich method with anti-GH IgG as the first antibody and chemiluminescent acridinium ester-labelled specific anti-GH F(ab′)2 as the second antibody. The measurable range of salmon GH in the CLIA was 39-1250 pg/mL using a short assay (1 day) protocol and 3.9-125 pg/mL in a longer (2-day) assay. The dilution curve in the CLIA of serum from masu salmon (Oncorhynchus masou) was parallel to the standard curve of recombinant chum salmon (Oncorhynchus keta) GH. Seasonal changes of serum GH levels were measured in 1 year-old masu salmon cultivated in a pond from March to November. Their serum GH levels increased during smoltification from March to April, achieved a maximum level of 21 ng/mL in August, and then declined gradually to 11 ng/mL in October. © 1997 John Wiley & Sons, Ltd.
    Additional Material: 3 Ill.
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  • 2
    Electronic Resource
    Electronic Resource
    Immune complex transfer two-site chemiluminescent immunoassay for serum growth hormone in alevin chum salmon (1998)
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 13 (1998), S. 107-111 
    Details
    ISSN: 0884-3996
    Keywords: chemiluminescent immunoassay ; acridinium ester ; fish ; salmon ; growth hormone ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: An immune complex transfer two-site chemiluminescent immunoassay (CLIA) for salmon growth hormone (GH) was developed to measure serum GH in alevin chum salmon (Oncorhynchus keta) using a chemiluminescent acridinium ester as a label. The immune complex transfer method dramatically reduced non-specifically bound of acridinium ester-labelled antibody without a decrease in the specific binding. Consequently, we could detect lower levels of GH than achieved previously in a two-site CLIA for salmon GH. The detection limit of the assay was 7.8 fg/mL and the standard curve was linear up to 250 fg/mL. Coefficients of variation were 2.2-7.7% within-assay and 5.3-9.1% between-assay. We have developed a highly sensitive and reproducible GH method and applied it to measurement of GH in alevin chum salmon. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 2 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    Affinity precipitation of α-amylase inhibitor from wheat meal by metal chelate affinity binding using cu(II)-loaded copolymers of 1-vinylimidazole with N-isopropylacrylamide (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 59 (1998), S. 695-704 
    Details
    ISSN: 0006-3592
    Keywords: immobilized metal affinity precipitation ; α-amylase inhibitor ; wheat ; poly(N-isopropylacrylamide) ; vinylimidazole ; iminodiacetic acid ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A method for purifying α-amylase inhibitor from wheat meal based on immobilized metal affinity with a thermosensitive copolymer is developed. The studies represent the thermoprecipitation properties of the copolymers of N-isopropylacrylamide (NIPAM) with iminodiacetic acid (IDA) and 1-vinylimidazole (VI), respectively. The polymer which is obtained by the copolymerization of 1-vinylimidazole and N-isopropylacrylamide, charged with Cu(II), exhibited specific interaction of the metal ions to the protein inhibitor. The precipitation was induced by salt and the recovery of the amylase inhibitor was achieved by dissolving the inhibitor-polymer complex in imidazole buffer and subsequent precipitation of the polymer. A single family of the α-amylase inhibitor was recovered from the polymer with 89% yield and about fourfold purification. The SDS-PAGE pattern showed significant purification of the inhibitor. The binding of the inhibitor to the Cu(II)-polymer conjugate depends upon the Cu(II) concentration in the copolymer and also upon the concentration of the protein. The recovered polymer could be reused with reasonable efficiency. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 59:695-704, 1998.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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