PRIMARY STRUCTURE OF THE MAJOR GLYCAN FROM HUMAN SEMINAL TRANSFERRIN

Citation
G. Dandrea et al., PRIMARY STRUCTURE OF THE MAJOR GLYCAN FROM HUMAN SEMINAL TRANSFERRIN, Journal of protein chemistry, 13(1), 1994, pp. 31-36
Citations number
18
Categorie Soggetti
Biology
ISSN journal
02778033
Volume
13
Issue
1
Year of publication
1994
Pages
31 - 36
Database
ISI
SICI code
0277-8033(1994)13:1<31:PSOTMG>2.0.ZU;2-R
Abstract
Human seminal transferrin (HSmT) is an iron-containing glycoprotein wh ose structural properties have not been adequately investigated. The c arbohydrate content of the purified glycoprotein amount to 6.1%, and m onosaccharide analysis revealed the major oligosaccharide moiety to be of the N-glycoside type. The carbohydrate chains were released from t he iron-free form by digestion with peptide N-glycosidase F (PNGase F) in the presence of detergents such as SDS and beta-octylglucoside. Af ter ethanol precipitation and fractionation on Bio-Gel P-6 and Bio-Gel P-2, the oligosaccharide was further purified on Mono-Q and desalted on Bio-Gel P-2. By 600-MHz H-1-NMR spectroscopy, the primary structure of the major N-linked oligosaccharide component was established to be : [GRAPHICS]