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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1999-3-18
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pubmed:abstractText |
Ara h 1, a major peanut allergen was isolated, and its structure on secondary, tertiary, and quaternary level at ambient temperature was investigated using spectroscopic and biochemical techniques. Ara h 1 appeared to be a highly structured protein on a secondary level, possesses a clear tertiary fold, and is present as a trimeric complex. Heat treatment of purified Ara h 1 results in an endothermic, irreversible transition between 80 and 90 degreesC, leading to an increase in beta-structures and a concomitant aggregation of the protein. Ara h 1 from peanuts that were heat-treated prior to the purification procedure exhibited a similar denatured state with an increased secondary folding and a decreased solubility. The effect of heat treatment on the in vitro allergenic properties of Ara h 1 was investigated by means of a fluid-phase IgE binding assay using serum from patients with a clinically proven peanut allergy. Ara h 1 purified from peanuts heated at different temperatures exhibited IgE binding properties similar to those found for native Ara h 1, indicating that the allergenicity of Ara h 1 is heat-stable. We conclude that the allergenicity of Ara h 1 is unaffected by heating, although native Ara h 1 undergoes a significant heat-induced denaturation on a molecular level, indicating that the recognition of conformational epitopes of Ara h 1 by IgE either is not a dominant mechanism or is restricted to parts of the protein that are not sensitive to heat denaturation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Allergens,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Ara h 1 protein, Arachis hypogaea,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin E,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4770-7
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:9988715-Adult,
pubmed-meshheading:9988715-Allergens,
pubmed-meshheading:9988715-Antigens, Plant,
pubmed-meshheading:9988715-Arachis hypogaea,
pubmed-meshheading:9988715-Calorimetry, Differential Scanning,
pubmed-meshheading:9988715-Chromatography, Gel,
pubmed-meshheading:9988715-Circular Dichroism,
pubmed-meshheading:9988715-Glycoproteins,
pubmed-meshheading:9988715-Hot Temperature,
pubmed-meshheading:9988715-Humans,
pubmed-meshheading:9988715-Immunoglobulin E,
pubmed-meshheading:9988715-Plant Proteins,
pubmed-meshheading:9988715-Protein Conformation,
pubmed-meshheading:9988715-Spectrophotometry, Ultraviolet
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pubmed:year |
1999
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pubmed:articleTitle |
Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties.
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pubmed:affiliation |
TNO Nutrition and Food Research Institute, 3700 AJ Zeist, The Netherlands. koppelman@voeding.tno.nl
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pubmed:publicationType |
Journal Article
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