Allergenic Characterization Of Soybean Proteins: Development Of A High Throughput Protein Microarray Immunoassay To Study The Allergenicity Of Proteins. Este artículo no está disponible.
Idioma: inglés
Editorial: Vdm Verlag Dr. Müller, 2010
- Tapa blanda
- Nuevo

Librería: Revaluation Books, Exeter, Reino UnidoRevaluation Books
Vendedor de 5 estrellas
Vendedor de IberLibro desde 6 de enero de 2003
No disponible
Tapa blanda
Condición: Nuevo
EUR 162,72
Descripción del artículo del vendedor
244 pages. 8.66x5.91x0.55 inches. In Stock.
N° de ref. del artículo 3639228820
- Título
- Allergenic Characterization Of Soybean Proteins: Development Of A High Throughput Protein Microarray Immunoassay To Study The Allergenicity Of Proteins
- Autor
- Lin, Jing; Fu, Zhiyan; Lin, Jing; Fu, Zhiyan
- Editorial
- Vdm Verlag Dr. Müller
- Año de publicación
- 2010
- Estado
- Brand New
- Encuadernación
- Paperback
- Idioma
- inglés
- ISBN 10
- 3639228820
- ISBN 13
- 9783639228823
- Peso del artículo
- 0,41 kilogramos
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.
“Sinopsis” puede pertenecer a otra edición de este título.
Reseña del editor
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.
“Acerca de” puede pertenecer a otra edición de este título.