ISSN:
1744-313X
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
,
Medicine
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1744-313X.1981.tb00769.x
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