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COMPOSITION AND IMMUNOCHEMICAL PROPERTIES OF GLYCOPROTEINS WITH ANTI‐B AGGLUTININ ACTIVITY ISOLATED FROM EUONYMUS SIEBOLDIANA SEEDS
Author(s) -
Yamamoto S.,
Sakai I.
Publication year - 1981
Publication title -
international journal of immunogenetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.41
H-Index - 47
eISSN - 1744-313X
pISSN - 1744-3121
DOI - 10.1111/j.1744-313x.1981.tb00769.x
Subject(s) - rhamnose , chemistry , size exclusion chromatography , biochemistry , agglutinin , fucose , mannose , chromatography , sepharose , concanavalin a , melibiose , galactose , lectin , glycoprotein , molecular mass , sucrose , maltose , in vitro , enzyme
Summary 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.