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Allergenic Characterization of Soybean Proteins: Development of a high throughput protein microarray immunoassay to study the allergenicity of proteins - Couverture souple

Lin, Jing; Fu, Zhiyan

 
9783639228823: Allergenic Characterization of Soybean Proteins: Development of a high throughput protein microarray immunoassay to study the allergenicity of proteins
Couverture souple
ISBN 10 : 3639228820 ISBN 13 : 9783639228823
Editeur : VDM Verlag Dr. Müller, 2010

Synopsis

The aim of the research presented in the book was to relate the structure of soybean 2 S albumins to their allergenicity. Using the methylotrophic yeast Pichia pastoris, two recombinant soybean 2 S albumins (rAL1 and rAL3) were produced as secreted proteins. Biophysical results indicated that the recombinant proteins were correctly folded and exhibited similar structures to those of the purified native soybean 2 S albumin (nAL3). Similarly to many plant allergens, these 2 S albumins were highly stable to pepsin digestion as well as heat and chemical treatment. In order to investigate whether the soybean 2 S albumins possess other biological activities that might have contributed to their allergenicity, several assays were carried out. The 2 S albumins from soybean appeared to affect the culture absorbance of two out of 10 species of fungi tested. Antimitotic studies have shown that nAL3 could also weakly inhibit cell division when microinjected into human HeLa cells. The ability of the soybean 2 S albumins to be recognized by IgEs from 23 European patients clinically characterized as allergic to soybean was determined using a novel high throughput protein microarray technique.

Les informations fournies dans la section « Synopsis » peuvent faire référence à une autre édition de ce titre.

Présentation de l'éditeur

The aim of the research presented in the book was to relate the structure of soybean 2 S albumins to their allergenicity. Using the methylotrophic yeast Pichia pastoris, two recombinant soybean 2 S albumins (rAL1 and rAL3) were produced as secreted proteins. Biophysical results indicated that the recombinant proteins were correctly folded and exhibited similar structures to those of the purified native soybean 2 S albumin (nAL3). Similarly to many plant allergens, these 2 S albumins were highly stable to pepsin digestion as well as heat and chemical treatment. In order to investigate whether the soybean 2 S albumins possess other biological activities that might have contributed to their allergenicity, several assays were carried out. The 2 S albumins from soybean appeared to affect the culture absorbance of two out of 10 species of fungi tested. Antimitotic studies have shown that nAL3 could also weakly inhibit cell division when microinjected into human HeLa cells. The ability of the soybean 2 S albumins to be recognized by IgEs from 23 European patients clinically characterized as allergic to soybean was determined using a novel high throughput protein microarray technique.

Biographie de l'auteur

Jing Lin: PhD in Life Science at The University of Nottingham, UK. Postdoctoral Fellow in Pediatric Allergy & Immunology at Mount Sinai School of Medicine, New York, NY, USA Zhiyan Fu: PhD, Director of Bioinformatics Cord Facility at The Wistar Institute, Philadelphia, PA, USA

Les informations fournies dans la section « A propos du livre » peuvent faire référence à une autre édition de ce titre.

Éditeur
VDM Verlag Dr. Müller
Date d'édition
2010
Langue
anglais
ISBN 10 
3639228820
ISBN 13 
9783639228823
Reliure
Broché
Nombre de pages
244
Coordonnées du fabricant
non disponible
Personne responsable
non disponible