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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4-5
|
| pubmed:dateCreated |
1996-8-9
|
| pubmed:databankReference | |
| pubmed:abstractText |
Pollen of Chamaecyparis obtusa (Japanese cypress) is one of the causes of allergic pollinosis in Japan. A major allergen of the pollen designated Cha o 1, was purified by two-step ion exchange chromatography. Cha o 1 was separated into four components with molecular masses of 48.5 kDa and 52.0 kDa, each with pIs of 6.77 and 6.82. The 23-residue N-terminal sequence of Cha o 1 was determined and shown to have high identity with that of Cry j 1, a major allergen of Cryptomeria japonica pollen. cDNA coding for Cha o 1 was cloned by hybridization screening using Cry j 1 cDNA as a probe. One of the cDNA clones, pCHA-1 was sequenced and found to code for a putative 21-residue signal peptide and a 354-residue native protein with a derived molecular mass of 38.1 kDa. The deduced amino acid sequence of Cha o 1 showed 79-80% identity with those of Cry j 1. These findings were consistent with observations of a close crossreaction between the two allergens. Homology analyses revealed that Cha o 1 had 46-49% identity with Amb a 1 families and Amb a 2, the major allergens of short ragweed. Cry j 1 has pectate lyase enzyme activity, suggesting that Cha o 1 may have the same enzyme activity as Cry j 1.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0161-5890
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
33
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
451-60
|
| pubmed:dateRevised |
2004-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:8676896-Allergens,
pubmed-meshheading:8676896-Amino Acid Sequence,
pubmed-meshheading:8676896-Base Sequence,
pubmed-meshheading:8676896-Blotting, Northern,
pubmed-meshheading:8676896-Cloning, Molecular,
pubmed-meshheading:8676896-Humans,
pubmed-meshheading:8676896-Molecular Sequence Data,
pubmed-meshheading:8676896-Molecular Weight,
pubmed-meshheading:8676896-Pollen
|
| pubmed:articleTitle |
Purification, characterization and molecular cloning of Cha o 1, a major allergen of Chamaecyparis obtusa (Japanese cypress) pollen.
|
| pubmed:affiliation |
Department of Otorhinolaryngology, Nagoya City University Medical School, Japan.
|
| pubmed:publicationType |
Journal Article
|