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pubmed-article:2097913pubmed:abstractTextA 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.lld:pubmed
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pubmed-article:2097913pubmed:authorpubmed-author:GarciaM AMAlld:pubmed
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pubmed-article:2097913pubmed:pagination17-24lld:pubmed
pubmed-article:2097913pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:2097913pubmed:articleTitleStructural studies on allergen RC-13 from Ricinus communis L.: isolation and characterization of a major glycopeptide.lld:pubmed
pubmed-article:2097913pubmed:affiliationDepartamento de Bioquímica, Universidade Federal do Rio de Janeiro.lld:pubmed
pubmed-article:2097913pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:2097913pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed