Antisera, rabbit, reactivity

A competitive enzyme immunoassay for the quantification of ivermectin residues in bovine liver has also been reported recently (85). This method uses a polyclonal antiserum raised in rabbits against 5-O-succinoylivermectin-trans-ferrin conjugate. Cross-reactivity was demonstrated with doramectin, a member... 

Figure 6. Reactivities of whole antiserum and purified anti-Gll and anti-Gn,b antibodies against liposomes containing glycolipids. Antibodies purified from rabbit anti-bovine brain ganglioside serum as described previously (12). Glucose release measured from liposomes containing DMPC, CHOL, DCP, and either Cm, Gpn CMH, CDH, DDG (each 150 p.g/ymol PC) or CTH (150 nmol/pmol PC).

Radioimmunoassay methods have been developed for pentazocine which were shown to be both sensitive and specific. An early method utilized tritium labeled pentazocine at 1.5 Ci/mmol. Antibodies were produced in rabbits to both an azoben-zoic acid and a carboxymethyl derivative of pentazocine coupled by carbodiimide condensation to poly-L-lysine. No cross reactivity was found for metabolites and benzomorphan analogs to the former antiserum with only conjugated pentazocine crossreacting with the latter antiserum (62). 

Antiserum specific for the biologically more active X-pentazocine has been produced in rabbits using an -pentazocine-2 -carboxymethyl ether-bovine serum albumin conjugate. A low 0.08 cross-reactivity was found for [Pg.391]

Complete, immunological cross-reactivity was demonstrated between components II and III with rabbit anti-component III antiserum, thereby providing strong evidence that the two molecular species are closely related.199... 

Maertlbauer et al. [34] developed a highly specific and sensitive enzyme immuno assay for the quantitative determination of natamycin in cheese rind. Rabbits were immunized with a natamycin-HSA conjugate to produce a specific antiserum. A labelled ligand was produced by coupling natamycin to horseradish peroxidase. The range of this ELISA test was between 0.2 and 2 ng per ml of sample solution. This allowed the determination of natamycin in cheese rind down to concentrations of 5 ng/dm2 or 0.1 mg/kg. The recovery in a range of 1 to 80 mg/kg was 76 to 84%. The cross-reactivity with amphotericin B and nystatin was <0.001%. 

Results of DEAE-anion exchange chromatography are shown in Figure 1. Partially purified BT israelensis crystal proteins (25 to 28 kilodalton peptides) were used in the immunization of rabbits. Western Blotting (Figure 2) showed that this antiserum reacted strongly with the 25- to 28- kDa peptides. Cross reactivity with the other BT israelensis crystal proteins and the BT kurstaki toxin was minimal. 

A number of enzyme-linked immunosorbent assay (ELISA) methods have also been reported. Koppelman et al. (2007) reported the development of ELISA methods to detect mustard protein contamination of mustard seed oil [6]. A rabbit polyclonal antiserum was raised to B.juncea and used to develop an inhibition ELISA assay with a reported detection limit of 1.5 ppm (mg/kg). Weak cross-reactivity with soy (0.016%) and milk (0.28%) was reported. 

ELISA Systems Mustard Seed Protein Residue kit was released in June 2007. A polyclonal rabbit antiserum was raised and used to develop a quantitative sandwich ELISA that has been demonstrated to detect mustard seed protein from aU three species of mustard plants S. alba, B. nigra, and B. juncea [5]. The detection limit of the kit has been shown to be less than 0.5 ppm (mg/kg) of soluble mustard protein, which corresponds to mustard seed concentrations below 3.4ppm S. alba, below 4.9 ppm B. nigra, and below 5.5 ppm B. juncea. An example of a calibration curve is presented in Figure 23.1. Cross-reactivity studies were conducted on full-strength extracts from 50 plants and other common foods, and cross-reactivity was observed only with rapeseed (Canola), Brassica napus. This cross-reactivity was approximately 50%, but purified canola oil did not cross react. 

Since most rabbit k chains have been identified either by amino acid sequence analysis or by their reactivity with anti-b-specific allotype sera, it is not known whether purely K-specific determinants (distinct from allotype-specific determinants) exist in these chains. To the authors knowledge, there has never been a report of a reaction between any k-specific antiserum and rabbit light chains. Very likely, it has not yet been looked for seriously. 

Pulmonary granuloma formation induced by infusion of 5 mg particulate glucan/rat was markedly reduced when neutrophils were depleted by rabbit antiserum directed against rat peripheral blood neutrophils or by catalase (15,000 U/raf) at the time of injection and 24 h after glucan infusion (Kilgore et al. 1997). Neutrophils and reactive oxygen intermediates (H2O2) are required for the local induction of monocyte attractant protein-1 to be secreted by endothelial cells. 

Proteins with lysine at position 190 are designated Oz(-l-) those with arginine are Oz(—). This substitution can be detected with an antiserum which gives a positive reaction only with Oz(-f) Bence Jones proteins (and with normal sera) (20). A rabbit antiserum which recognizes the presence of glycine at position 152 has also been developed reactive proteins, designated Kem(-I-), comprised 8 of 38 monoclonal X chains studied (21a). 

Immunological cross-reactivity with human IgA was demonstrated initially for the serum and secretory immunoglobulins of the dog, cat, horse, cow, sheep, pig, goat, hedgehog, rabbit, and mouse, as well as of primates. The use of chicken rather than mammalian antiserum proved particularly valuable for demonstrating cross-reactions (105). No cross-... 

A more extensive investigation of immunological cross-reactivity of mammalian IgA s was subsequently reported by Neoh et al. (105a), who utilized in their tests sheep, goat, rabbit, and chicken antisera specific for human IgA. A protein cross-reacting with human IgA was identified in the plasma of nearly all of the more than 90 mammalian species tested. The chicken antiserum was especially useful for demonstrating reactivity of nonprimate IgA. Among the relatively few species whose sera failed to react with anti-IgA were several artiodactyls (big horned sheep, antelope, etc.). In view of the diversity of mammalian species in which IgA has been identified it seems reasonable to extrapolate to the conclusion that it may be present in all mammals (104). 

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