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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0024530,
umls-concept:C0030956,
umls-concept:C0055782,
umls-concept:C0086418,
umls-concept:C0205470,
umls-concept:C0220781,
umls-concept:C0439849,
umls-concept:C0445223,
umls-concept:C0871161,
umls-concept:C1552599,
umls-concept:C1704787,
umls-concept:C1708096,
umls-concept:C1883254,
umls-concept:C2603343
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pubmed:issue |
6
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pubmed:dateCreated |
1989-10-20
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pubmed:abstractText |
A glycine-linked tetramer of Asn-Ala-Asn-Pro, a tandem repeated sequence of malaria circumsporozoite (CS) protein, was synthesized by the Boc-based solid phase method, followed by deprotection with 1 M trimethylsilyl trifluoromethanesulfonate-thioanisole in trifluoroacetic acid. In addition, three tetramer-related peptides were similarly synthesized, i.e., a 34-residue peptide [linked with TH, a proposed T-cell epitope of CS, at the C-terminus of the tetramer], a 46-residue peptide and a 59-residue peptide [linked with HA or HA', two proposed T-cell epitopes of influenza hemagglutinin protein, at the N-terminus of the above 34-residue peptide]. Their immunological properties were examined by enzyme-linked immunosorbent assay, for which three different congenic strains of mouse were used to raise the specific antibodies. Despite conjugation of T-cell epitopes to the tetramer, the mice of low-responder strains to the tetramer failed to produce any antibody specific to the tetramer. However, with the aid of recombinant interleukin 2 as an adjuvant, the low-responder mice produced antibody with relatively high titers.
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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 |
Jun
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pubmed:issn |
0009-2363
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1612-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading | |
pubmed:year |
1989
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pubmed:articleTitle |
Studies on peptides. CLXVII. Solid-phase syntheses and immunological properties of fragment peptides related to human malaria circumsporozoite protein.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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