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Antibodies chicken

Kennedy et developed an immunoassay for salinomycin and utilized the lA to check the depletion of salinomycin in chicken muscle and liver. The limit of quantitation was 0.31 pgkg for muscle and 0.29 pgkg for liver these levels were based on the assay response of negative samples -I- 6 SD. The antibody cross-reacted with narasin but did not recognize lasalocid, maduramicin, and monensin. [Pg.705]

Kennedy et al. developed a lasalocid immunoassay for application to residues in chicken meat and liver samples. The antibody was specific and did not cross-react with salinomycin, maduramicin, or monensin. Sample preparation consisted of homogenization in aqueous acetonitrile, removal of fat from an aliquot of the aqueous acetonitrile by hexane extraction, and evaporation of acetonitrile. The sample was then reconstituted with assay buffer. Liver required an additional solid phase extraction step. The LOQ was 0.02 xgkg for muscle and 0.15 agkg for liver. These workers were able to use the system to determine the half-life of lasalocid in the tissues. [Pg.706]

Hamada, S., Senzaki, K., Hamaguchi-Hamada, K. et al. (1998). Localization of 5-HT2a receptor in rat cerebral cortex and olfactory system revealed by immuno-histochemistry using two antibodies raised in rabbit and chicken. Molec. Brain Res. 54, 199-211. [Pg.271]

Primary antibody incubation. Prepare primary antibody cocktail in the blocking buffer (5% normal horse serum, buffer + azide), and incubate 1 h at room temperature. We typically use a mix of mouse, rabbit, goat, and/or chicken primary antibodies together see Table 5.2 for appropriate dilutions of the recommended antibodies. At this point (or during secondary antibody incubation), it is usually safe to incubate the samples overnight at 4°. [Pg.108]

Infectious bronchitis virus (IBV) SI glycoprotein Potato tuber Antibodies neutralized IBV from mice and chickens. Immunogenic in chickens when administered orally, nasally, and parenterally. Protective after 3 immunizations in chickens when challenged with virulent IBV. 103... [Pg.146]

Antibodies raised against venom of various spiders Specificity against toxin of Clostridium tetani Specificity against toxin of C. tetani Antibodies against tick-borne encephalitis virus Specificity for causative agent of chicken pox... [Pg.374]

Significant exposure to chicken pox or shingles for patients who have no history of either condition or, if available, negative antibody to VZV... [Pg.460]

Immunosuppressive effects have been obtained in vitro with mercuric chloride. A marked inhibition of the mixed lymphocyte reaction in mice as well as PFC (plaque forming cell) response to SRBC (sheep red blood cells) by mercuric chloride [166] has been reported. Chronic exposure to mercury of rabbits gave immunosuppression, measured as low antibody titres to viral agents [167], A suppression of antibody production in chickens exposed to mercuric chloride has also been reported [168]. Furthermore, an inhibition of mitogenic response to PHA in lymphocytes by mercuric chloride has been obtained [169],... [Pg.201]

Alternatively, GFP can be visualized using rabbit polyclonal antibody raised against GFP purified directly from A. victoria. This anti-GFP antibody facilitates the detection of native GFP, recombinant GFP, and GFP-fusion proteins both by immunofluorescence and brightfield microscopy, as well as by western blot analysis and immunoprecipitation. Direct anti-GFP conjugates made from a complete serum or from an IgG fraction are available from Invitrogen (http //www.invitrogen.com/ site/us/en/home.html). Additional options for your research offered by Invitrogen include two mouse monoclonal antibodies and a chicken IgY fraction. [Pg.96]

Many different types of lesions have been observed (very often at autopsy) in animals suffering from severe pantothenic acid deficiency. These may involve the skin, the adrenals, the entire gastrointestinal tract, nerves, and spinal cord. Functionally, in chickens fertility may be reduced by pantothenic acid deficiency to practically zero64 without any outward signs being shown by the fowls. Recently, pantothenic acid deficiency has been found to produce duodenal ulcers in about 60 per cent of the rats tested.65 It is required for bone development66 and is implicated in antibody responses.67... [Pg.201]

Dichlorodiphenyltrichloroethane (DDT) Increased susceptibility for infection (chicken, duck) Reduced antibody responses (rabbit)... [Pg.441]

Seo et al. (1999) used a planar optic biosensor that measures the phase shift variation in refractive index due to antigen binding to antibody. In this method, they were able to detect S. enterica serovar T) himurium with a detection limit of 1 x 10 cfu/ml. When chicken carcass fluid was inoculated with 20 cfu/ml, the sensor was able to detect this pathogen after 12 h of nonselective enrichment. A compact fiber optic sensor was also used for detection of S. T) himurium at a detection limit of 1 X 10" cfu/ml (Zhou et al., 1997, 1998) however, its efficacy with food samples is unproven. Later, Kramer and Lim (2004) used the fiber optic sensor, RAPTOR , to detect this pathogen from spent irrigation water for alfalfa sprouts. They showed that the system can be used to detect Salmonella spiked at 50 cfu/g seeds. An evanescent wave-based multianalyte array biosensor (MAAB) was also employed for successful testing of chicken excreta and various food samples (sausage, cantaloupe, egg, sprout, and chicken carcass) for S. T) himurium (Taitt et ah, 2004). While some samples exhibited interference with the assay, overall, the detection limit for this system was reported to be 8 x 10 cfu/g. [Pg.12]

While invertebrate tropomyosins are likely pan-allergens, vertebrate tropomyosins appear to be nonallergenic (Reese et ah, 1999). Using bioinformatics approaches to compare the sequences of tropomyosins from various species, Goodman et ah (2002) determined that tropomyosins from vertebrate species — rabbit, pig, chicken, and human — share 53-57% amino acid sequence identity to the known shrimp tropomyosin allergen. Met e 1. This comparison likely explains why vertebrate tropomyosins are not allergenic and do not cross-react with IgE antibodies specific to invertebrate tropomyosins. [Pg.161]

Schade R, Behn I, Erhard M, Hlinak A, Staak C (eds.) (2001) Chicken egg yolk antibodies, production and application. Springer, Berlin Wild D (2005) The immunoassay handbook. Elsevier, Oxford... [Pg.129]


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See also in sourсe #XX -- [ Pg.291 ]




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