CONJUGATES OF CARBOHYDRATE CHAINS OF ALPH A(1)-ACID GLYCOPROTEIN WITHPOLYACRYLAMIDE RETAIN THE IMMUNOMODULATING ACTIVITY

Translocation of carbohydrate glycoprotein N-chains onto soluble polya crylamide was proposed as a method for studying the biological role of carbohydrate chains. N-linked carbohydrate chains of alpha1-acid glyc oprotein (AGP) were aminated at the reducing GlcNAc moiety and covalen tly attached to polyacrylamide (PAA). Thus ''pseudo-AGP'' was obtained where peptide core was replaced with PAA. The synthetic model mimics AGP by M(r) and carbohydrate content as well as the ratio of tetra-, t ri- and diantennary and mono-, di-, tri- and tetrasialo chains. It was shown that the conjugate inhibits proliferation of lymphocytes like t he parent AGP. Therefore, the property of AGP to inhibit the lymphocyt e proliferation is attributed to its carbohydrate chains, whereas pept ide core serves as carrier providing polyvalent interaction of multipl e carbohydrate chains with cell.