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.
Indian J Biochem Biophys
;
1980 Feb; 17(1): 24-31
Article
in English
| IMSEAR
| ID: sea-29047
3.
Indian J Biochem Biophys
;
1978 Dec; 15(6): 449-55
Article
in English
| IMSEAR
| ID: sea-28115
4.
Indian J Biochem Biophys
;
1977 Jun; 14(2): 129-31
Article
in English
| IMSEAR
| ID: sea-26840
Subject(s)
Animals , Glycopeptides/isolation & purification , Glycoproteins/analysis , Rats , Skin/analysis , Sodium Chloride
5.
Indian J Biochem Biophys
;
1976 Jun; 13(2): 141-4
Article
in English
| IMSEAR
| ID: sea-29157
6.
Indian J Biochem Biophys
;
1974 Jun; 11(2): 141-3
Article
in English
| IMSEAR
| ID: sea-28006