scholarly journals Identification of Immunoglobulin E-Binding Proteins of the Xerophilic Fungus Aspergillus penicillioides Crude Mycelial Mat Extract and Serological Reactivity Assessment in Subjects with Different Allergen Reactivity Profiles

2018 ◽  
Vol 175 (3) ◽  
pp. 147-159
Author(s):  
Joenice González De León ◽  
Ricardo González Méndez ◽  
Carmen L. Cadilla ◽  
Félix E. Rivera-Mariani ◽  
Benjamín Bolaños-Rosero
Keyword(s):  
Binding Proteins ◽  
Immunoglobulin E ◽  
Serological Reactivity

scholarly journals Immunoglobulin E-binding Proteins of Cooked Walnuts in Korean Children

2018 ◽  
Vol 10 (4) ◽  
pp. 363 ◽  
Author(s):  
Jeongmin Lee ◽  
Kyunguk Jeong ◽  
Se-ah Jeon ◽  
Sooyoung Lee
Keyword(s):  
Binding Proteins ◽  
Immunoglobulin E ◽  
Korean Children

scholarly journals A helix-loop-helix protein related to the immunoglobulin E box-binding proteins.

1990 ◽  
Vol 10 (8) ◽  
pp. 4384-4388 ◽  
Author(s):  
C S Carr ◽  
P A Sharp
Keyword(s):  
Transcription Factor ◽  
Binding Site ◽  
Heavy Chain ◽  
Binding Proteins ◽  
Immunoglobulin E ◽  
Expression Library ◽  
Helix Loop Helix ◽  
E Box ◽  
Late Transcription ◽  
Novel Protein

A human cDNA encoding a novel protein in the helix-loop-helix family has been isolated by screening a bacteriophage expression library with a probe containing the binding site for major late transcription factor. The protein encoded by this cDNA, TFEB, probably recognizes E-box sequences in the heavy-chain immunoglobulin enhancer.

A helix-loop-helix protein related to the immunoglobulin E box-binding proteins

1990 ◽  
Vol 10 (8) ◽  
pp. 4384-4388
Author(s):  
C S Carr ◽  
P A Sharp
Keyword(s):  
Transcription Factor ◽  
Binding Site ◽  
Heavy Chain ◽  
Binding Proteins ◽  
Immunoglobulin E ◽  
Expression Library ◽  
Helix Loop Helix ◽  
E Box ◽  
Late Transcription ◽  
Novel Protein

A human cDNA encoding a novel protein in the helix-loop-helix family has been isolated by screening a bacteriophage expression library with a probe containing the binding site for major late transcription factor. The protein encoded by this cDNA, TFEB, probably recognizes E-box sequences in the heavy-chain immunoglobulin enhancer.

Food allergy to wheat: differences in immunoglobulin E-binding proteins as a function of age or symptoms

2005 ◽  
Vol 42 (1) ◽  
pp. 109-117 ◽  
Author(s):  
Fabrice Battais ◽  
Philippe Courcoux ◽  
Yves Popineau ◽  
Gisèle Kanny ◽  
Denise Anne Moneret-Vautrin ◽  
...  
Keyword(s):  
Food Allergy ◽  
Binding Proteins ◽  
Immunoglobulin E

A Recombinant ω-Gliadin-like D-Type Glutenin and an α-Gliadin from Wheat (Triticum aestivum): Two Immunoglobulin E Binding Proteins, Useful for the Diagnosis of Wheat-Dependent Allergies

2012 ◽  
Vol 60 (32) ◽  
pp. 8059-8068 ◽  
Author(s):  
Hamza Mameri ◽  
Isabelle Bouchez ◽  
Catherine Pecquet ◽  
Nadia Raison-Peyron ◽  
Dominique Choudat ◽  
...  
Keyword(s):  
Triticum Aestivum ◽  
Binding Proteins ◽  
Immunoglobulin E

Probiotic Preparation Has the Capacity To Hydrolyze Proteins Responsible for Wheat Allergy

2007 ◽  
Vol 70 (1) ◽  
pp. 135-144 ◽  
Author(s):  
MARIA DE ANGELIS ◽  
CARLO G. RIZZELLO ◽  
ENRICO SCALA ◽  
CLAUDIO DE SIMONE ◽  
GIOVANNI A. FARRIS ◽  
...  
Keyword(s):  
Experimental Design ◽  
Wheat Flour ◽  
Binding Proteins ◽  
Immunoglobulin E ◽  
Sodium Dodecyl ◽  
Baker’S Yeast ◽  
Baker's Yeast ◽  
Gut Colonization ◽  
Ige Binding ◽  
Sds Page

This study was aimed at showing the capacity of probiotic VSL#3 to hydrolyze wheat flour allergens. Hydrolysis was investigated either by the use of baker's yeast bread treated with digestive enzymes and VSL#3, an experimental design that mimicked the activity of probiotics during gut colonization, or by the use of VSL#3 as a starter for dough fermentation, an experimental design that mimicked the predigestion of wheat flour proteins during food processing. Albumins, globulins, and gliadins extracted from wheat flour and chemically acidified and started dough and total proteins extracted from breads were analyzed by immunoblotting with pooled sera from patients with an allergy to wheat. Hydrolysis of wheat flour proteins was determined by sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) and two-dimensional electrophoresis (2DE). Mass spectrometry matrix-assisted laser desorption and ionization–time of flight was used to identify some immunoglobulin E (IgE)–binding proteins. As shown by immunoblotting with sera from allergic patients, several IgE-binding proteins persisted after treatment of baker's yeast bread by pepsin and pancreatin. The signal of all these IgE-binding proteins disappeared after further treatment by VSL#3. As shown by SDS-PAGE and related immunoblotting and 2DE analyses, when VSL#3 was used as a starter for bread making, it caused a marked degradation of wheat proteins, including some IgE-binding proteins such as the putative transcription factor APFI and wheat α-amylase inhibitors. Indeed, the IgE-binding profile of the bread manufactured by VSL#3 was largely different from that of baker's yeast bread. The IgE-binding proteins that persisted in the bread made with VSL#3 were completely degraded by pepsin and pancreatin.

High resolution spot scan imaging of frozen, hydrated actin bundles with 400kV electrons

1992 ◽  
Vol 50 (1) ◽  
pp. 512-513
Author(s):  
J. Jakana ◽  
M.F. Schmid ◽  
P. Matsudaira ◽  
W. Chiu
Keyword(s):  
High Resolution ◽  
Binding Proteins ◽  
Actin Binding ◽  
Eukaryotic Cells ◽  
Dimensional Structure ◽  
Structural Basis ◽  
Actin Bundle ◽  
Actin Bundles ◽  
3 Dimensional ◽  
Macromolecular Assembly

Actin is a protein found in all eukaryotic cells. In its polymerized form, the cells use it for motility, cytokinesis and for cytoskeletal support. An example of this latter class is the actin bundle in the acrosomal process from the Limulus sperm. The different functions actin performs seem to arise from its interaction with the actin binding proteins. A 3-dimensional structure of this macromolecular assembly is essential to provide a structural basis for understanding this interaction in relationship to its development and functions.

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