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

S.D.Shiyan, A.L.Pukhalsky, A.P.Toptygina, V.V.Nasonov, N.V.Bovin
Conjugates of the carbohydrate chains of the α1-acid glycoprotein with polyacrylamide retain the immunomodulating activity of the natural glycoprotein. [Article in Russian]
Russ. J. Bioorgan. Chem., 20 (8-9), pp. 994 - 1000, (1994)

Translocation of carbohydrate glycoprotein N-chains onto soluble polyacrylamide was proposed as a method for studying the biological role of carbohydrate chains. N-linked carbohydrate chains of α1-acid glycoprotein (AGP) were aminated at the reducing GlcNAc moiety and covalently attached to polyacrylamide (PAA). Thus "pseudo-AGP" was obtained where peptide core was replaced with PAA. The synthetic model mimics AGP by Mr and carbohydrate content as well as the ratio of tetra-, tri- and diantennary and mono-, di-, tri- and tetrasialo chains. It was shown that the conjugate inhibits proliferation of lymphocytes like the parent AGP. Therefore, the property of AGP to inhibit the lymphocyte proliferation is attributed to its carbohydrate chains, whereas peptide core serves as carrier providing polyvalent interaction of multiple carbohydrate chains with cell.

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