Antibodies reaction with denatured protein

Several groups have created multifunctional streptavidins with reversible linkers to solid surface. Scouten and Konecny [87] used an immobilized oligonucleotide to capture a biotinylated complementary oligonucleotide bound to streptavidin, which was free to react with biotinylated protein. A captured biotinylated antibody was released by denaturation of the duplex DNA by incubation at low ionic strength. Morris and Rany [88] reported the release of streptavidin bound to the 3 (but not the 5 ) end in an ATP-dependent helicase reaction. 

Reactions of ozone with proteins can be observed in vitro as well as in vivo [14, 16]. The primary reaction of ozone with egg albumin is similar to its denaturation. Changes of the UV-light absorption, particularly in the tyrosine spectrum, and a reduced solubility occur. These structural changes are sufficient to induce the production of antibodies when the ozonized proteins are injected into rabbits. The exposure of rabbits to an environment containing 10 ppm ozone for one hour weekly for six weeks induced the formation of antibodies in the blood serum in detectable... 

Precise information on antigenic determinants reactive in T-cell activation, delayed hypersensitivity, and other manifestations of cellular immunity is quite limited. What has clearly emerged, however, is the notion that B- and T-cells react normally or at least frequently to different determinants on the same molecule. The classical example is that of Gell and Benacerraf (1959), where heat-denatured proteins lost their capacity to react with antibody against the native protein, whereas delayed reactions could be provoked with either native or denatured antigen. This finding was open to at least two possible interpretations namely that cellular immunity has a broader specificity than antibody responses, or that the structural entities serving as determinants in humoral and cellular immunity are not the same. 

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