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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1988-12-20
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pubmed:abstractText |
A purified preparation of a major allergen of Japanese cedar pollen, sugi basic protein (SBP, Cry j I), was separated into 5 subfractions of 50-45 kDa. All of the SBP subfractions were confirmed to be reactive to IgE antibodies from patients with Japanese cedar pollinosis, and also to mouse anti-SBP monoclonal antibodies. The sequences of 20 N-terminal amino acids of these 5 subfractions were found to be identical. Peptide mapping analyses of the SBP subfractions showed similar patterns, with some differences which might in part be due to the existence of an N-linked carbohydrate chain. The N-terminal amino acid sequence of SBP was identical to the reported sequence of an allergen of mountain cedar which vegetated in North America.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
239
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
329-32
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pubmed:dateRevised |
2000-12-18
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pubmed:meshHeading | |
pubmed:year |
1988
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pubmed:articleTitle |
N-terminal amino acid sequence of a major allergen of Japanese cedar pollen (Cry j I).
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pubmed:affiliation |
Hayashibara Biochemical Laboratories, Inc., Okayama, Japan.
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pubmed:publicationType |
Journal Article
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