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Allergens proteins and

Barletta, B., Di Felice, G., Pini, C. 2007. Biochemical and molecular biological aspects of silverfish allergens. Protein and Peptide Letters 14(10) 970-974. [Pg.252]

Alcocer, M.J., Murtagh, G.J., Bailey, K. et al. 2002. The disulphide mapping, folding and characterisation of recombinant Ber e 1, an allergenic protein, and SFA8, two sulphur-rich 2S plant albumins. J Mol Biol 324 165-175. [Pg.263]

Nakamura, R. and Matsuda, T. 1996. Rice allergenic protein and molecular-genetic approach for hypoallergenic rice. Biosci Biotech Biochem 60 1215-1221. [Pg.332]

Because allergenic food proteins are responsible for the sensitization and elicitation of allergic reactions, most detection methods have been based on the detection of these proteins. Alternatively, DNA has been suggested as a target for the detection of allergenic material in food. However, its use has been a controversial topic because the correlation between the presence of allergenic protein and DNA in processed food may not be constant. At least four factors may affect this correlation ... [Pg.176]

Other techniques for the bioanalytical characterisation of allergenic proteins and for the elucidation of the tertiary stmcture are nuclear magnetic resonance spectroscopy and x-ray structure analysis, in which separated or purified proteins are used. The two techniques are still the only methods available for a determination of the stmcture of macromolecules such as proteins and nucleic acid on an atomic level, but are usually not utilized in standard food analysis. Both methods have been employed successfully in the elucidation of allergenic proteins [33,34]. [Pg.355]

For applications where surgical gloves provide adequate protection, if these are of natural rubber latex tlien powder-free gloves witli low/undetectable protein and allergen levels are advisable. (Alternatively the use of nitrile gloves eliminates the risk of latex allergy.)... [Pg.437]

We performed collaborative studies using the ELISA methods with model processed foods (sausage, boiled beef in an aluminum pouch, tomato sauce, biscuit, juice, and jam) containing allergen proteins. The six... [Pg.156]

Fig. 12.5. Schematic summary of the eight T. canis proteins containing predicted SXC (NC6) domains. The consensus is shown in the N-terminal domain of PEB-1 (phosphatidylethanolamine-binding protein-1) as xCxDxxxDC(6x)C(11x) RCxxTCxxC. This consensus is faithfully repeated in MUC-1 (mucin-1), MUC-2, MUC-4 and MUC-5, and in all but the C-terminal domain of MUC-3. This domain (and the C-terminal SXC domain of PEB-1) show consensus spacing but some variation in consensus residues. Two additional proteins with quadrupled SXC domains differ in spacing between cysteines-2, -3 and -4, and show more variation in consensus residues. These are VAH-1 (venom allergen homologue) and HUF-001 (homologue of unknown function-001). Fig. 12.5. Schematic summary of the eight T. canis proteins containing predicted SXC (NC6) domains. The consensus is shown in the N-terminal domain of PEB-1 (phosphatidylethanolamine-binding protein-1) as xCxDxxxDC(6x)C(11x) RCxxTCxxC. This consensus is faithfully repeated in MUC-1 (mucin-1), MUC-2, MUC-4 and MUC-5, and in all but the C-terminal domain of MUC-3. This domain (and the C-terminal SXC domain of PEB-1) show consensus spacing but some variation in consensus residues. Two additional proteins with quadrupled SXC domains differ in spacing between cysteines-2, -3 and -4, and show more variation in consensus residues. These are VAH-1 (venom allergen homologue) and HUF-001 (homologue of unknown function-001).
Antibodies have been used extensively as diagnostic tools in many different formats, especially for measurement of protein and cytokine abundances. Applications of antigen arrays can be found in reverse immunoassays for detection of allergens and autoimmune antibodies. [Pg.479]

In summary, it is reasonable to conclude that bioinformatic analysis of structural similarities to, or of sequence homology with, known protein allergens, and evaluation of stability with SGF, can both contribute, if interpreted cautiously, to an overall assessment of sensitizing hazard. However, these analyses, neither alone nor in combination, provide a definitive answer regarding allergenic potential, and for this reason there has been interest in exploring a more holistic approach (and more definitive assessment) that may be provided by suitable animal models. [Pg.614]

Ivanciuc, O., Schein, C.H. and Braun, W., SDAP Database and computational tools for allergenic proteins. Nucleic Acids Res., 31, 359, 2003. [Pg.620]

Fu, T.J., Abbott, U. And Hatzos, C., Digestibility of food allergens and non-allergenic proteins in simulated gastric and intestinal fluids — a comparative study. J. Agric. Food Chem., 50, 7154, 2002. [Pg.620]

Hilton, J., Dearman, R.J., Basketter, D.A. and Kimber, I., Serological responses induced in mice by immunogenic proteins and by protein respiratory allergens. Toxicol. Lett., 73,43,1994. [Pg.622]


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See also in sourсe #XX -- [ Pg.4 , Pg.37 ]

See also in sourсe #XX -- [ Pg.4 , Pg.37 ]




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