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
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