Purification and characterization of recombinant Bet v I, the major birch pollen allergen. Immunological equivalence to natural Bet v I.-Reference-Cited by-同舟云学术

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Purification and characterization of recombinant Bet v I, the major birch pollen allergen. Immunological equivalence to natural Bet v I.

Published:1993-09 Issue:26 Volume:268 Page:19574-19580
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Ferreira F.D.,Hoffmann-Sommergruber K,Breiteneder H,Pettenburger K,Ebner C,Sommergruber W,Steiner R,Bohle B,Sperr W.R.,Valent P

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference51 articles.

1. In Vivo Half-Life of a Protein Is a Function of Its Amino-Terminal Residue

2. Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure

3. Analysis of recombinant proteins by isoelectric focusing in immobilized pH gradients

4. The gene coding for the major birch pollen allergen Betv1, is highly homologous to a pea disease resistance response gene.

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1. Genetic variability of the major birch pollen allergen Bet v 1 and characterization of B- and T-cell epitopes;Doklady of the National Academy of Sciences of Belarus;2024-09-06

2. Experience of allergen-specific immunotherapy in the patient with oral and systemic manifestations of birch pollen allergy;Allergology and Immunology in Paediatrics;2024-06-24

3. Tree-Pollen-Related Food Allergies: Birch Pollen and More;Current Treatment Options in Allergy;2023-11-16

4. Description and Clinical Exposure of Allergic Plants;Pollen Allergy in a Changing World;2023

5. L’acérola, un fruit exotique riche en vitamine C contient une LTP allergénique;Revue Française d'Allergologie;2022-11

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