Source:http://linkedlifedata.com/resource/pubmed/id/11267676
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
2001-3-27
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pubmed:databankReference | |
pubmed:abstractText |
A cDNA clone encoding a soybean allergen, Gly m Bd 28K, has been isolated. The clone has a 1567-bp cDNA insert with a 1419-bp open reading frame and a 148-bp 3'-untranslated region, followed by a polyadenylation tail. The open reading frame was shown to encode a polypeptide composed of 473 amino acids. The chemically determined amino acid sequences of the peptides obtained from the allergen, including its N-terminal peptide, were shown to be contained in the N-terminal region of the amino acid sequence deduced from the cDNA, showing that the first half of the cDNA encodes the allergen with a preceding segment of 21 amino acids. The peptide fragment including the allergen was expressed as a fusion protein with glutathione S-transferase in Escherichia coli and immunoblotted with the sera of soybean-sensitive patients and the monoclonal antibody against the allergen. Furthermore, homology analyses demonstrate that the polypeptide for the cDNA exhibits high homology with the MP27/MP32 proteins in pumpkin seeds and the carrot globulin-like protein. This finding suggests that the polypeptide may consist of a 21-amino acid segment as a part of the signal peptide and the proprotein, which may be converted to two mature proteins, Gly m Bd 28K and a 23-kDa protein, during the development of soybean cotyledons.
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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/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Gly m Bd 28K allergen, Glycine max,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Soybean Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
1518
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
178-82
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:11267676-Allergens,
pubmed-meshheading:11267676-Amino Acid Sequence,
pubmed-meshheading:11267676-Antigens, Plant,
pubmed-meshheading:11267676-Base Sequence,
pubmed-meshheading:11267676-Cloning, Molecular,
pubmed-meshheading:11267676-DNA, Complementary,
pubmed-meshheading:11267676-Glycoproteins,
pubmed-meshheading:11267676-Molecular Sequence Data,
pubmed-meshheading:11267676-Open Reading Frames,
pubmed-meshheading:11267676-Plant Proteins,
pubmed-meshheading:11267676-Sequence Homology, Amino Acid,
pubmed-meshheading:11267676-Soybean Proteins,
pubmed-meshheading:11267676-Soybeans
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pubmed:year |
2001
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pubmed:articleTitle |
Cloning of cDNA encoding a soybean allergen, Gly m Bd 28K.
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pubmed:affiliation |
Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University, Juboki 111, Soja 719-1197, Japan. htsuji@fhw.oka-pu.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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