PURIFICATION AND PROPERTIES OF SESAME LECTIN
摘要
A protein with the properties of a lectin has been isolated from Sesame indicumL.in pure form by affinity chromatography on a chitin column.Gel electrophoresisin sodium dodecyl sulfate gave a single protein band with molecular weight about56,000.The gel stained with periodic acid-Schiff reagent,indicating bound carbohy-drate.As the lectin was split into two polypeptide chains of molecular weights about30,000 and 26,000 on reduction with 2-mercaptoethanol,the presence of inter-chain disulfide bonds is indicated.Studies on the carbohydrate-binding specificityshowed that the lectin may be specific towards N-acetylglucosamine from the factthat the lectin can bind specifically and reversibly with chitin,the polysaccharides ofN-acetylglucosamine,and form a precipitin line with hyaluronic acid or heparinby the double diffusion technique.The lectin agglutinated human red blood cellswithout discrimination among blood groups.It also agglutinated rabbit erythrocytesas well as mouse spleen cells.Treatment of erythrocytes with trypsin greatlyincreased agglutinability by the sesame lectin.