PURIFICATION AND PHYSICHEMICAL CHARACTERIZATION OF A LECTIN FROM WISTARIA SINENSIS SWEET

A lectin from Wistaria sinensis has been purified respectively from the solution of crude extract by DEAE-C ion-exchange chromatographic column. The DEAE-C ion-exchange chromatographic column has been treated by ordinary methods and the lectin is eluted from the column by a linear ionie strength gradient. The hemagglutination activity of the purified lectin showed an activity increase of 40 fold for rabbit erythrocytes.The recovery of total activity was 19.2%.The molecular weight of the lectin from Wistaria sinensis is 205kd as determined by PAGE.The lectin molecule is a tetramer which consists of two kind of subunits and each kind of subunits has two.The molecular weights of these subunits are 77600d and 25100d as determined by SDS PAGE.The lectin from Wistaria sinensis a kind of glycoprotein.The isoelectric point of the lectin is 4.60.The lectin can agglutinate the erythocytes of each human blood group and of some animals, but it is nonspecific.The hemagglutination activity is inhibited by many saccharidesand it can be inhibited mostly by N-acetyl-D-galactosamine.Amino acid analysis shows that the lectin molecule contained relatively more Glu,Asp and less Cys-Cys, Pro, Tyr.