Anti-dinitrophenyl antibodies

Antibodies Affinity labeling of antibody combining sites as illustrated by anti-dinitrophenyl antibodies, 46, 479 p-azoben-zenearsonate antibody, 46, 492 affinity cross-linking of heavy and light chains, 46, 501 bivalent affinity labeling haptens in the formation of model immune complexes, 46, 505 DNP-based diazoketones and azides, 46, 508 labeling of antilactose antibody, 46, 516. 

Since the photoisomerizable dinitrospiropyran units tethered to the redox enzyme act as photoisomerizable antigen sites for the anti-dinitrophenyl antibody DNP-Ab, the light-controlled association and dissociation of the antibody to and from the antigen-functionalized redox enzyme layer may control the bioelectrocatalytic functions... 

The enzymatic back-filling immunoassay model has been demonstrated with the dinitrophenyl antigen-functionalized surface and anti-dinitrophenyl antibody as target analyte... 

D. Bassolino-Klimas, R. E. Bruccoleri, S. Subramaniam. Modeling the antigen combining site of an anti-dinitrophenyl antibody, AN02. Protein Sci. 1992, 1, 1465-1476. 

Anti-dinitrophenyl antibodies Anti-(egg albumin) antibody... 

JV-2,4-DinitrophenyI- alanine Anti-dinitrophenyl antibody Heavy chain labeled 36... 

N-t- (4-Azido-2-nitro-phenyl)lysine Binding site of anti-dinitrophenyl antibody Heavy chain labeled between 29 and 34 and 95 and 114 (i.e., two of the hypervariable regions) 107... 

Affinity Labeling of Antibody Combining Sites as Illustrated by Anti-Dinitrophenyl Antibodies... 

Tatsu et a/.(106) reported a novel immunosensor using immobilized liposomes doped with carboxyfluorescein and dinitrophenyl (DNP) hapten on the tip of an optical fiber. On complement-mediated immunolysis by anti-DNP-antibody, the fluorescent signal of the liberated carboxyfluorescein was measured. 

M. M. Timbs, C. L. Poglitsch, M. L. Pisarchick, M. T. Sumner, and N. L. Thompson, Binding and mobility of anti-dinitrophenyl monoclonal-antibodies on fluid-like, langmuir-blodgett phospholipid monolayers containing dinitrophenyl-conjugated phospholipids, Biochim. Biophys. Acta 1064, 219— 228(1991). 

M. Mammen, F. A. Gomez, and G. M.Whitesides, Determination of the binding of ligands containing the N-2,4 dinitrophenyl group to bivalent monoclonal rat anti-DNP antibody using affinity capillary electrophoresis, Anal. Chem. 67, 3526-3535 (1995). 

An enzyme immunoassay using adenosine deaminase as the enzyme label has been described (318). Potentiometric rate measurements were made with an ammonia gas-sensing electrode. The immunoassay system employed is based on competition between a model haptenic group, dinitrophenyl (DNP) covalently coupled to adenosine deaminase, and free DNP hapten for the available binding sites on the anti-DNP antibody molecules. The detection limit is 50 ng antibody. 

After blotting of the proteins, they are dinitrophenylated (Section 12.5). This hapten is then detected with anti-DNP antibodies (Miles, Inc.j by one of the methods discussed below. Detectability by this method is at least equal to that of autoradiography (< 1 ng). The intensity of the staining, however, is not representative of the stoichiometry of the protein in the blot. Kittler et al. (1984) haptenated the amino groups of the blotted proteins with pyridoxal-5 -phosphate. This method requires no organic solvents and can also be used with Zetabind membranes. 

Isolation by immunoadsorption of anti-(2,4-dinitrophenyl) antibody preparations Purification of low molecular weight Factor VIII Separation of heparin into functionally distinct fractions investigation of mechanism of action of heparin... 

The immune complex transfer assay has allowed the development of very sensitive EIAs for the detection of antibodies. In one example, the assay utilizes a 2,4-dinitrophenyl (DNP)-biotin-conjugated antigen. This is incubated with the sample antibody to be measured, and, after the immune reaction, the immune complexes are trapped onto a primary solid phase coupled with anti-DNP antibody. After washing away unbound materials, immune complexes are eluted with DNP-lysine and transferred to a secondary streptavidin-coated solid phase. Next, an enzyme-labeled anti-immunoglobulin antibody is added, and, after washing, enzyme activity is assayed. In this case, the enzyme activity correlates with the amount of antibody in the sample. The sensitivity depends on the amount of nonspecific binding of the enzyme-labeled antibody on the second solid phase. Thus, several modified assay systems have been developed to reduce background. 

Purification of specific anti-(2,4-dinitrophenyl) antibodies by immunoadsorption Purification of Datura stramonium phytohaemagglutinin by affinity chromatography Affinity chromatography of Phaseolus vulgaris phytohaemaglutinin... 

Binding of Some 2,4-Dinitrophenyl (Dnp) Derivatives by Rabbit Anti-Dnp Antibodies" ... 

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