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  • 1
    Electronic Resource
    Electronic Resource
    Homogeneous immunoassay of polyclonal antibodies by use of antigen-coupled liposomes (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 41 (1993), S. 862-867 
    Details
    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
    URL: http://dx.doi.org/10.1002/bit.260410905
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Reaction characteristics and stability of a membrane-bound enzyme reconstituted in bilayers of liposomes (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 37 (1991), S. 809-813 
    Details
    ISSN: 0006-3592
    Keywords: Membrane-bound enzyme ; Reconstitution ; Liposome ; Immobilization ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effects ensuing from the interaction between membrane-bound sarcosine dehydrogenase and the surrounding lipids as well as the effects of membrane fluidity were described in this study. A 25-fold activation was observed upon the reconstitution of the enzyme in bilayers of SUVs made of DMPC. The considerable decrease in Km and increase in Vmax suggest the induction of favorable conformational changes in both the substrate-binding site and the catalytic site of the enzyme due to the lipid-protein interaction. In SUVs of negatively charged phospholipids, the enzyme retained its initial activity over 1 month. The break point in the Arrhenius plot of the activity of reconstituted enzyme was found at temperatures close to the gel-liquid crystalline transition point of the phospholipid showing that the activity is sensitive to the physical state of membrane phospholipids. Further, immobilization of the reconstituted enzyme by use of ENT prepolymer resulted in a high activity, whereas no remarkable activity was detected with the immobilized enzyme without reconstitution.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260370904
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    Paper (German National Licenses)
    Fulltext
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