Source:http://linkedlifedata.com/resource/pubmed/id/15508178
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2004-10-27
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pubmed:abstractText |
All novel proteins must be assessed for their potential allergenicity before they are introduced into the food market. One method to achieve this is the 2001 FAO/WHO Decision Tree recommended for evaluation of proteins from genetically modified organisms (GMOs). It was the aim of this study to investigate the allergenicity of microbial transglutaminase (m-TG) from Streptoverticillium mobaraense. Amino acid sequence similarity to known allergens, pepsin resistance, and detection of protein binding to specific serum immunoglobulin E (IgE) (RAST) have been evaluated as recommended by the decision tree. Allergenicity in the source material was thought unlikely, since no IgE-mediated allergy to any bacteria has been reported. m-TG is fully degraded after 5 min of pepsin treatment. A database search showed that the enzyme has no homology with known allergens, down to a match of six contiguous amino acids, which meets the requirements of the decision tree. However, there is a match at the five contiguous amino acid level to the major codfish allergen Gad c1. The potential cross reactivity between m-TG and Gad c1 was investigated in RAST using sera from 25 documented cod-allergic patients and an extract of raw codfish. No binding between patient IgE and m-TG was observed. It can be concluded that no safety concerns with regard to the allergenic potential of m-TG were identified.
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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/Immune Sera,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin E,
http://linkedlifedata.com/resource/pubmed/chemical/Pepsin A,
http://linkedlifedata.com/resource/pubmed/chemical/Transglutaminases,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1613-4125
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
48
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
434-40
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pubmed:dateRevised |
2007-3-22
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pubmed:meshHeading |
pubmed-meshheading:15508178-Animals,
pubmed-meshheading:15508178-Consumer Product Safety,
pubmed-meshheading:15508178-Cross Reactions,
pubmed-meshheading:15508178-Decision Trees,
pubmed-meshheading:15508178-Food Hypersensitivity,
pubmed-meshheading:15508178-Gadus morhua,
pubmed-meshheading:15508178-Humans,
pubmed-meshheading:15508178-Immune Sera,
pubmed-meshheading:15508178-Immunoglobulin E,
pubmed-meshheading:15508178-Organisms, Genetically Modified,
pubmed-meshheading:15508178-Pepsin A,
pubmed-meshheading:15508178-Risk Assessment,
pubmed-meshheading:15508178-Sequence Homology, Amino Acid,
pubmed-meshheading:15508178-Streptomyces,
pubmed-meshheading:15508178-Transglutaminases,
pubmed-meshheading:15508178-Trypsin
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pubmed:year |
2004
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pubmed:articleTitle |
Evaluation of the potential allergenicity of the enzyme microbial transglutaminase using the 2001 FAO/WHO Decision Tree.
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pubmed:affiliation |
Laboratory of Medical Allergology, Allergy Clinic, National University Hospital, Copenhagen, Denmark.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Evaluation Studies
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