Aug 1, 1981

Composition and immunochemical properties of glycoproteins with anti-B agglutinin activity isolated from Euonymus sieboldiana seeds

Journal of Immunogenetics
S Yamamoto, I Sakai


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 micrograms/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.

Mentioned in this Paper

Galactose Measurement
Blood Group H Type 1 Antigen
Amino Acids, I.V. solution additive
Red blood cells, blood product
Chromatography, DEAE-Cellulose

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