COMPOSITION AND IMMUNOCHEMICAL PROPERTIES OF GLYCOPROTEINS WITH ANTI‐B AGGLUTININ ACTIVITY ISOLATED FROM EUONYMUS SIEBOLDIANA SEEDS

Five major glycoproteins with anti‐B agglutinin activity were isolated from seeds of Euonymus Sieboldiana by a procedure based on precipitation with ammonium sulphate, Sepharose 4B gel filtration, CM‐ and DEAE‐Sepharose chromatography and Sephacryl S‐200 gel filtration. The purified glycoproteins each gave a single symmetrical peak on Sephacryl S‐200 gel filtration with elution volumes corresponding to molecular weights of approximately 15,000 to 130,000, each forming a single precipitin line on gel diffusion plates with anti‐E. Sieboldiana antibody. These anti‐B glycoproteins were rich in acidic amino acids without cysteine and methionine and contained about 8‐36% carbohydrate, of which galactose, arabinose and glucose were the predominant sugars, with small amounts of glucosamine, rhamnose, fucose, xylose, mannose and ribose. The most anti‐B active lectin agglutinated human B red blood cells at a concentration of 2 μg/ml and was strongly inhibited by melibiose. The three other lectins with anti‐B agglutinin activity, however, were not inhibited by any galactose‐containing glycosides.