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Titolo:
N-terminal sequences of high molecular weight allergens from celery tuber
Autore:
Ganglberger, E; Radauer, C; Grimm, R; Hoffmann-Sommergruber, K; Breiteneder, H; Scheiner, O; Jensen-Jarolim, E;
Indirizzi:
Univ Vienna, Neubau AKH, Dept Gen & Expt Pathol, A-1090 Vienna, Austria Univ Vienna Vienna Austria A-1090 & Expt Pathol, A-1090 Vienna, Austria Hewlett Packard Co, Chem Anal Grp Europe, Waldbronn, Germany Hewlett Packard Co Waldbronn Germany nal Grp Europe, Waldbronn, Germany
Titolo Testata:
CLINICAL AND EXPERIMENTAL ALLERGY
fascicolo: 4, volume: 30, anno: 2000,
pagine: 566 - 570
SICI:
0954-7894(200004)30:4<566:NSOHMW>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
CROSS-REACTIVE ALLERGEN; BIRCH POLLEN ALLERGENS; PLANT-DERIVED FOOD; MAJOR ALLERGEN; IDENTIFICATION; MUGWORT; PURIFICATION; SENSITIVITY; PROFILIN; API-G-1;
Keywords:
Api g 5; birch pollen; celery; cross-reactive allergen;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
17
Recensione:
Indirizzi per estratti:
Indirizzo: Jensen-Jarolim, E Univ Vienna, Neubau AKH, Dept Gen & Expt Pathol, EBO-3Q,Wahringer Gurtel 18-20, A-1090 Vienna, Austria Univ Vienna EBO-3Q,WahringerGurtel 18-20 Vienna Austria A-1090
Citazione:
E. Ganglberger et al., "N-terminal sequences of high molecular weight allergens from celery tuber", CLIN EXP AL, 30(4), 2000, pp. 566-570

Abstract

Background Celery tuber is an important source of food allergens. Low molecular weight celery allergens were identified as homologues of Bet v 1 and profilin. Little is known about the relevant allergens with molecular weights between 45 and 60 kDa, which cross-react with other plant food and pollen allergens. Objective The aim of this study was to isolate cross-reactive, high molecular weight allergens from celery and to characterize them by N-terminal sequencing. Methods High molecular weight allergens of celery were identified by immunoglobulin (Ig) E immunoblotting with patients' sera, and the IgE-binding patterns were compared with those of the monoclonal antibirch pollen antibodyBIP3, as well as of a polyclonal rabbit anti-Art v 1 antiserum. Two independent methods, elution from preparative SDS-PAGE or anion exchange chromatography, were used to purify the IgE-binding celery proteins of interest. The isolated proteins were examined by N-terminal sequencing and IgE-immunoblots. Results Celery allergens with molecular masses of 55, 58 and 63 kDa, whichwere also recognized by the monoclonal BIP3 antibody and a polyclonal anti-Art v 1 antiserum, were isolated. The 63-kDa allergen was N-terminally blocked. The 55- and 58-kDa compounds yielded the same N-terminus, which showed no homology to known proteins in the databases. Conclusion The combination of two independent protein separation techniques, immunoblotting and N-terminal sequencing, identified an N-terminus of two allergens in the 60-kDa molecular weight region. Our data will be helpfulfor the definite molecular characterization of these important cross-reactive molecules.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/11/18 alle ore 03:42:20