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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 613 (1990), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 41 (1993), S. 862-867 
    ISSN: 0006-3592
    Keywords: homogenous immunoassay ; polyclonal antibody ; lysis of liposome ; complement system ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Anti-cytochrome c and anti-myoglobin antibodies were assayed by use of immunoliposomes coupled with the antigens. Addition of complement under the existence of the antigens. Addition of complement under the existence of the antigen-antibody complex on the surface of the liposome caused lysis of the liposomes, which was proportional to the amount of the antigen-antibody complex formed as well as the concentration of complement added. Thus, the degree of marker release depended on the average association constant and also on its heterogeneity of the polyclonal antibodies, which shows that the results assayed by this method are correlated to the antibody ability to form the antigen-antibody complex © 1993 Wiley & Sons, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 34 (1989), S. 532-540 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Immunoadsorbents were modified with monomethoxy-polyethylene glycol (PEG; average molecular weights of 5000 (PEG-5000) and 1900 (PEG-1900)) activated with cyanuric acid (activated PEG) by four different methods. In the two methods, anti-BSA antibodies were modified with activated PEG with and without protection of antigen binding sites with BSA and then were coupled to CNBr-activated Sepharose 4B. In the other two methods, Immunoadsorbents, which were prepared by coupling anti-BSA antibodies to CNBr-activated Sepharose 4B, were modified with activated PEG with and without the protection. The effects of PEG modification by these four methods on the binding ratio (the ratio of the numbers of moles of antigen adsorbed to the numbers of moles of binding sites of antibody coupled), the antigen binding property and the resistance to proteolytic digestion of immunoadsorbents were studied. The decrease in the binding ratio by the modification with activated PEG was small enough to use modified immunoadsorbents for industrial purification processes. The resistance to proteolytic digestion of immunoadsorbents was improved by modification with activated PEG. The modification without protection of antigen binding sites gave higher resistance to proteolytic digestion than that with protection, while the former caused larger decrease in the binding ratio of modification. The immunoadsorbents modified with activated PEG-5000 showed higher resistance to proteolytic digestion than those modified with activated PEG-1900.
    Additional Material: 14 Ill.
    Type of Medium: Electronic Resource
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