Antibody interactions

Fig. 9. Immunosensor approaches where A is the analyte, is the labeled analyte, and Y is the antibody, (a) Direct immunosensors where the actual antigen—antibody interaction is measured (b) indirect immunosensors 1 and 2 which utilize formats similar to competitive and displacement

HAp coatings, 14 105 HapMap project, 20 839 Hapten-antibody interactions, 9 64 Haptic sensor, for skin conditions, 3 749 Harcros antifoam, commercial defoamer, 3 24 It 

Immunoaffinity chromatography utilizes the high specificity of antigen—antibody interactions to achieve a separation. The procedure typically involves the binding, to a soHd phase, of a mouse monoclonal antibody which reacts either directly with the protein to be purified or with a closely associated protein which itself binds the product protein. The former approach has been appHed in the preparation of Factor VIII (43) and Factor IX (61) concentrates. The latter method has been used in the preparation of Factor VIII (42) by immobilization of a monoclonal antibody to von WiHebrand factor [109319-16-6] (62), a protein to which Factor VIII binds noncovalenfly. Further purification is necessary downstream of the immunoaffinity step to remove 

Ovary, Z., Immediate reactions in the skin of experimental animals provoked by antigen-antibody interactions, Progr. Allergy, 5, 460, 1958 

Liposome conjugates may be used in various immunoassay procedures. The lipid vesicle can provide a multivalent surface to accommodate numerous antigen-antibody interactions and thus increase the sensitivity of an assay. At the same time, it can function as a vessel to carry encapsulated detection components needed for the assay system. This type of enzyme-linked immunosorbent assay (ELISA) is called a liposome immunosorbent assay or LISA. One method of using liposomes in an immunoassay is to modify the surface so that it can interact to form biotin-avidin or biotin-streptavidin complexes. The avidin-biotin interaction can be used to increase detectability or sensitivity in immunoassay tests (Chapter 23) (Savage et al., 1992). 

Odorico, M., Teulon, J.-M., Bessou, T., Vidaud, C., Bellanger, L., Chen, S.-W., Qucmcncur, fi., Parot, P., and Pellequer, J.-L. (2007) Energy landscape of chelated uranyl Antibody interactions by dynamic force spectroscopy. Biophys. J. 93, 645-654. 

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