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Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia
[print version]

S.D.Shiyan, V.V.Nasonov, N.V.Bovin, L.I.Novikova, V.A.Aleshkin
The molecular forms of human α1-acid glycoprotein. Variations in the occurance of bi-, tri-, and tetraantennary N-linked carbohydrate chains.
Bioorgan. Khim., 17 (5), pp. 663 - 670, (1991)

α1-Acid glycoprotein isolated from healthy individuals blood was separated on Con A-Sepharose into three fractions: non-bound (AGP-1, 84%, 43.5 kDa), Con A-bound (AGP-2, 14%, 41.3 kDa), and Con A-tightly bound (AGP-3, 2%, 39.6 kDa). Amino acid compositions of these fractions were similar but carbohydrate ones differed. HPLC analysis of 7-amino-4-methylcoumarin derivatives of the oligosaccharides in combination with their sequential exoglycosidase digestion showed that AGP-1, AGP-2, and AGP-3 have the same set of oligosaccharides and differ only by their proposition. A minor quantity of agalacto-oligosaccharides (with a terminal GlcNAc residue) was identified.

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