INVESTIGADORES
WUNDERLIN Daniel Alberto
artículos
Título:
Analysis of IgE binding of Celtis tala pollen
Autor/es:
BARONI, M.V.; ALVAREZ, J.S.; WUNDERLIN, D. A.; CHIABRANDO, G. A.
Revista:
FOOD AND AGRICULTURAL IMMUNOLOGY
Editorial:
Routledge (Taylor and Francis)
Referencias:
Lugar: USA; Año: 2008 vol. 19 p. 187 - 194
ISSN:
0954-0105
Resumen:
Celtis tala (C. tala) is a tree, widely distributed in Argentina. Its significance as a source of allergic sensitisation is still unclear. Our aim was to partially characterise the IgE binding proteins of C. tala pollen. Skin prick tests using C. tala pollen extract were carried out in 25 patients with respiratory allergy. C. tala extract elicited positive skin reactions in five patients. Sensitised patients showed increased specific IgE levels to C. tala by immunodot. Immunoblotting assay demonstrated IgE binding to proteins of 50 kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen tala by immunodot. Immunoblotting assay demonstrated IgE binding to proteins of 50 kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen reactions in five patients. Sensitised patients showed increased specific IgE levels to C. tala by immunodot. Immunoblotting assay demonstrated IgE binding to proteins of 50 kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen tala by immunodot. Immunoblotting assay demonstrated IgE binding to proteins of 50 kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen carried out in 25 patients with respiratory allergy. C. tala extract elicited positive skin reactions in five patients. Sensitised patients showed increased specific IgE levels to C. tala by immunodot. Immunoblotting assay demonstrated IgE binding to proteins of 50 kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen tala by immunodot. Immunoblotting assay demonstrated IgE binding to proteins of 50 kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen reactions in five patients. Sensitised patients showed increased specific IgE levels to C. tala by immunodot. Immunoblotting assay demonstrated IgE binding to proteins of 50 kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen tala by immunodot. Immunoblotting assay demonstrated IgE binding to proteins of 50 kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen of allergic sensitisation is still unclear. Our aim was to partially characterise the IgE binding proteins of C. tala pollen. Skin prick tests using C. tala pollen extract were carried out in 25 patients with respiratory allergy. C. tala extract elicited positive skin reactions in five patients. Sensitised patients showed increased specific IgE levels to C. tala by immunodot. Immunoblotting assay demonstrated IgE binding to proteins of 50 kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen tala by immunodot. Immunoblotting assay demonstrated IgE binding to proteins of 50 kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen reactions in five patients. Sensitised patients showed increased specific IgE levels to C. tala by immunodot. Immunoblotting assay demonstrated IgE binding to proteins of 50 kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen tala by immunodot. Immunoblotting assay demonstrated IgE binding to proteins of 50 kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen carried out in 25 patients with respiratory allergy. C. tala extract elicited positive skin reactions in five patients. Sensitised patients showed increased specific IgE levels to C. tala by immunodot. Immunoblotting assay demonstrated IgE binding to proteins of 50 kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen tala by immunodot. Immunoblotting assay demonstrated IgE binding to proteins of 50 kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen reactions in five patients. Sensitised patients showed increased specific IgE levels to C. tala by immunodot. Immunoblotting assay demonstrated IgE binding to proteins of 50 kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen tala by immunodot. Immunoblotting assay demonstrated IgE binding to proteins of 50 kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen is a tree, widely distributed in Argentina. Its significance as a source of allergic sensitisation is still unclear. Our aim was to partially characterise the IgE binding proteins of C. tala pollen. Skin prick tests using C. tala pollen extract were carried out in 25 patients with respiratory allergy. C. tala extract elicited positive skin reactions in five patients. Sensitised patients showed increased specific IgE levels to C. tala by immunodot. Immunoblotting assay demonstrated IgE binding to proteins of 50 kDa and 55 kDa. C. tala pollen extract is allergenically potent requiring approximately 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these results taken together indicate that proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen proteins of 50 kDa and 55 kDa may be considered as specific allergens of C. tala pollen 50 ng of self-protein for 50% inhibition of IgE binding in ELISA inhibition, whereas no cross-inhibition was detected with other types of pollen widely distributed in Argentina (Helianthus annuus and Prosopis spp.). Thus, these r