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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1991-7-19
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pubmed:abstractText |
A glycoprotein, RC-13, isolated from Ricinus communis seeds was reduced, S-alkylated and cleaved by trypsin. The tryptic digest was fractionated by ion-exchange chromatography and a glycopeptide was isolated and purified by high-voltage paper electrophoresis. When submitted to amino acid and carbohydrate analyses this major glycopeptide showed the following chemical composition: Lys1, Asp1, Thr2, Ser4, Glu1, Pro2, Gly2, Ala2, Val2, GlcN6, Man6 and Gal8. Hydrazynolysis positioned Ser as the C-terminal residue. It is postulated that this glycopeptide belongs to the C-terminal region of the allergen.
|
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0001-3765
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
62
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
17-24
|
pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading | |
pubmed:year |
1990
|
pubmed:articleTitle |
Structural studies on allergen RC-13 from Ricinus communis L.: isolation and characterization of a major glycopeptide.
|
pubmed:affiliation |
Departamento de Bioquímica, Universidade Federal do Rio de Janeiro.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|