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Antibodies against haptens

In early studies, antibodies against haptens covalently linked to ends of the 16S RNA were used to locate the 3 end of 16S RNA on the upper "platform" of the 30S subunit (Fig. 29-1A).5160 The 5 terminus was found in the lower body. Two N6,N6-dimethyl-... [Pg.1686]

The reaction product 136 is not an appropriate hapten for generating catalytic antibody as it does not closely resemble the reaction intermediate 135. Antibody 1E9 was prepared against hapten 137, a stable analog of 135, and the catalyst promoted the Diels-Alder reaction with multiple (> 50) turnovers. [Pg.184]

Fig. 5 Chemical structure of the hapten conjugated to BSA used as immunogen by Roberts et al. [158] and Meyer et al. [154] to raise antibodies against dexamethasone. Structures of other corticosteroids subsequently tested by Creaser et al. [180] in order to evaluate the selectivity of the ELISA obtained are also shown... Fig. 5 Chemical structure of the hapten conjugated to BSA used as immunogen by Roberts et al. [158] and Meyer et al. [154] to raise antibodies against dexamethasone. Structures of other corticosteroids subsequently tested by Creaser et al. [180] in order to evaluate the selectivity of the ELISA obtained are also shown...
Scheme 48 Reagents and conditions i) polyclonal antibody raised against hapten (57). Scheme 48 Reagents and conditions i) polyclonal antibody raised against hapten (57).
Figure 2. Theozymes for hydroxyepoxide cyclizations. Antibody-catalyzed cyclization reactions are shown schematically in the box. Antibodies 26D9 and 5C8 were raised against haptens 4 and 5, respectively, (a) Theozymes (bold) complexed to the 6-endo cyclization transition state model. Figure 2. Theozymes for hydroxyepoxide cyclizations. Antibody-catalyzed cyclization reactions are shown schematically in the box. Antibodies 26D9 and 5C8 were raised against haptens 4 and 5, respectively, (a) Theozymes (bold) complexed to the 6-endo cyclization transition state model.
Fig. 9 Three haptens, [15]—[17], containing a 1,2-aminoalcohol functionality were investigated as alternatives for esterase and amidase induction. Of antibodies raised against hapten [15], 50% were shown to catalyse the hydrolysis of ester [18], thereby establishing the necessity for a compact haptenic structure. Hapten [19] along with [16] was employed in a heterologous immunization programme to elicit both a general and acid/base function in the antibody binding site. Fig. 9 Three haptens, [15]—[17], containing a 1,2-aminoalcohol functionality were investigated as alternatives for esterase and amidase induction. Of antibodies raised against hapten [15], 50% were shown to catalyse the hydrolysis of ester [18], thereby establishing the necessity for a compact haptenic structure. Hapten [19] along with [16] was employed in a heterologous immunization programme to elicit both a general and acid/base function in the antibody binding site.
Table 4 Kinetic parameters for those antibodies raised against phosphonates [88-91] which effect the resolution of the fluorinated alcohols [84-87]. The configuration of the disastereoisomerically pure product from each antibody-catalysed process was shown to correspond to that of the antibody-inducing hapten. Table 4 Kinetic parameters for those antibodies raised against phosphonates [88-91] which effect the resolution of the fluorinated alcohols [84-87]. The configuration of the disastereoisomerically pure product from each antibody-catalysed process was shown to correspond to that of the antibody-inducing hapten.
Fig. 32 Antibody AA71.17 raised against hapten [95] catalyses the hydrolysis of the... Fig. 32 Antibody AA71.17 raised against hapten [95] catalyses the hydrolysis of the...
Although small molecules do not usually stimulate antibody formation, antibodies against them can usually be raised if the small molecule, or hapten, is covalently attached to a large immunologically active carrier protein. [Pg.304]

Following the first successful examples of catalytic antibodies raised against haptens as transition state analogues (TSAs) reported by Lerner and Schultz, the TSA approach has been applied in a large number of studies in order to generate new biocatalysts for many chemical transformations. According to the transition state theory, the catalytic efficiency ( cat/ uncat) of given enzymatic reaction can be deduced from the thermodynamic cycle (Scheme 1) under ideal conditions. ... [Pg.325]

Figure 5 Tandem cationic cyclization catalyzed by antibody HA519A4 raised against hapten 4. Figure 5 Tandem cationic cyclization catalyzed by antibody HA519A4 raised against hapten 4.
Figure 6 Tandem cationic cyciization cataiyzed by antibody 4C6 raised against hapten 5. Figure 6 Tandem cationic cyciization cataiyzed by antibody 4C6 raised against hapten 5.
Figure 12 Oxy-Cope reaction catalyzed by antibody AZ28 raised against the hapten y and X-ray structure of the antibody AZ28-hapten y complex. Figure 12 Oxy-Cope reaction catalyzed by antibody AZ28 raised against the hapten y and X-ray structure of the antibody AZ28-hapten y complex.
Figure 15 Hydrolysis of phosphodiester bonds catalyzed by antibody MATT.F-1 raised against hapten 19 according to the bait and switch strategy. Figure 15 Hydrolysis of phosphodiester bonds catalyzed by antibody MATT.F-1 raised against hapten 19 according to the bait and switch strategy.
Figure 18 Kinetic resoiution of racemic naproxen ester 28 by antibody 15G2 raised against hapten 27. Figure 18 Kinetic resoiution of racemic naproxen ester 28 by antibody 15G2 raised against hapten 27.
Figure 20 Aldolization and retro-aldolization reactions catalyzed by antibodies raised against hapten 31. Figure 20 Aldolization and retro-aldolization reactions catalyzed by antibodies raised against hapten 31.
Immunopharmacotherapy has recently appeared as a viable treatment strategy for cocaine abuse using an animal model for relapse. Larsen et al were the first to construct a monoclonal antibody, GNC92H2, that was raised against hapten GNC (Figure 27(a)), and that was found to bind selectively to cocaine with respect to its metabolites with a of 10 mol 1 (Figure 27(b)). [Pg.346]

T4. Tanaka, K., Kohno, T, Hashida, S., and Ishikawa, E., Novel and sensitive noncompetitive (two-site) enzyme immunoassay for h tens with amino groups. J. Clin. Lab. Anal. 4,208—212(1990). T5. Towbin, H., Motz, J., Oroszlan, R, and Zingel, O., Sandwich immunoassay for the hapten angiotensin II. A novel assay principle based on antibodies against immune complexes. J. Immunol. Methods 181, 167-176 (1995). [Pg.170]


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See also in sourсe #XX -- [ Pg.122 , Pg.343 ]




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