SEPARATION OF SOLUBLE GLYCOPROTEINS FROM SUGARCANE JUICE BY CAPILLARY-ELECTROPHORESIS

Two different pools of glycoproteins, tentatively described as high an d mid-molecular mass polymers, are currently separated by conventional gel filtration. Anion-exchange chromatography on DEAE-Sephadex A-60 d iscriminates between neutral or cationic, and anionic polymers composi ng both fractions. The occurrence of both cationic and anionic glycopr oteins has been corroborated after separation by capillary electrophor esis. Total or partial digestion of the glycosidic moiety of these gly coproteins using beta-1,2-fructofuranosidase reveals that cationic spe cies from the mid molecular mass glycoproteins move to the neutral or anionic zone of the electropherogram whereas only one cationic form fr om high molecular mass polymers remains unchanged after enzymatic hydr olysis of the glycosidic moiety. This indicates that this moiety is ab le to modify the net charge of some of the mid-molecular mass glycopro teins whereas the net charge of cationic high molecular mass polymer c an be due to the own protein moiety or, probably, to some polycationic polyamines bound on this moiety. (C) 1998 Elsevier Science B.V. All r ights reserved.