Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Isolation and partial characterization of Fes p 4 allergen
Autore:
Gavrovic-Jankulovic, M; Cirkovic, T; Bukilica, M; Fahlbusch, B; Petrovic, S; Jankov, RM;
Indirizzi:
Univ Belgrade, Fac Chem, Dept Biochem, YU-11000 Belgrade, Yugoslavia Univ Belgrade Belgrade Yugoslavia YU-11000 YU-11000 Belgrade, Yugoslavia
Titolo Testata:
JOURNAL OF INVESTIGATIONAL ALLERGOLOGY & CLINICAL IMMUNOLOGY
fascicolo: 6, volume: 10, anno: 2000,
pagine: 361 - 367
SICI:
1018-9068(200011/12)10:6<361:IAPCOF>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
BASIC GLYCOPROTEIN ALLERGEN; PRATENSE POLLEN ALLERGENS; TIMOTHY PHLEUM-PRATENSE; GRASS-POLLEN; MONOCLONAL-ANTIBODIES; MAJOR ALLERGEN; EXTRACTS; EXPRESSION; REACTIVITY; ISOFORMS;
Keywords:
IgE reactivity; Fes p 4; glycoprotein; Festuca pratensis; grass group-4 pollen allergen; monoclonal antibody;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Gavrovic-Jankulovic, M Univ Belgrade, Fac Chem, Dept Biochem, Studentski Trg 16, YU-11000 Belgrade, Yugoslavia Univ Belgrade Studentski Trg 16 Belgrade Yugoslavia YU-11000
Citazione:
M. Gavrovic-Jankulovic et al., "Isolation and partial characterization of Fes p 4 allergen", J INVES ALL, 10(6), 2000, pp. 361-367

Abstract

More than 75% of grass pollen-allergic patients produce specific IgE antibodies against group-4 allergens. Purification and characterization of different grass group-4 allergens should help to further understand their allergenicity. In this study, an attempt was made to isolate and characterize Fesp 4 allergen by several biochemical and immunochemical methods. Fes p 4 was purified by a combination of chromatographic techniques (gel permeation and ion exchange chromatography). Isolated protein revealed four main spots at a molecular weight of 60 kDa and a pi ranging from 8.7 to 9.1. Eight sera were selected from patients with positive result of skin prick test to the mixture of grass pollen extracts. ELISA inhibition technique was used to study Fes p 4-specific IgE in the patients' sera. ELISA to Festuca pratensis was inhibited up to 80% by F. pratensis pollen extract and up to 48% by Fes p 4. 2D-PAGE-immunoblot was used to identify allergenic and antigenic components of Fes p 4 with patients' IgE and monoclonal antibodies (MABs). Three components of purified protein expressed IgE binding ability. Two MABs which recognized unrelated regions on Phl p 4 bound three components of Fesp 4. The role of the carbohydrate moiety in allergenicity was examined with individual patient sera by using periodate-treated Fes p 4. Six out of eight patients reduced IgE binding to periodate-treated allergen. Isolated Fes p 4 glycoprotein consisted of four components, three of which were allergenic, and share common epitopes specific for grass group-4 homologs. The results of periodate oxidation of Fes p 4 suggest that the carbohydrate moiety is involved in IgE binding.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/10/20 alle ore 12:17:14