1.
An. acad. bras. ciênc
;
62(1): 17-24, mar. 1990. tab
Article
in English
| LILACS
| ID: lil-92236
ABSTRACT
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
Subject(s)
Allergens/isolation & purification , Amino Acids/analysis , Ricinus communis/analysis , Glycopeptides/isolation & purification , Seeds/analysis , Peptide Mapping
2.
Partial characterization of RC-13, a homogenous fraction isolated from castor bean allergens (CB-1A)
An. acad. bras. ciênc
;
59(3): 149-53, set. 1987. tab, ilus
Article
in English
| LILACS
| ID: lil-47641
3.
An. acad. bras. ciênc
;
56(3): 323-31, 1984.
Article
in English
| LILACS
| ID: lil-20349