Proceeding
Some Properties of β-Galactose-binding Lectin Isolated from Fruiting Body of Agaricus blazei
1999 Volume 16 Pages 111-117
Details
1999 Volume 16 Pages 111-117
Beta D-galactose binding lectin was purified from the phosphate-saline (PBS) extract of fruiting body of Agaricus blazei by precipitation with 0.6 sat. ammonium sulfate follwed by affinity chromatography on either asiaofetuin-. N-acetyllactosamine or β-aminoethyl D-galactosidesepharose column, and gel filtration. The purified lectin consists of tetrametric glycopeptides with subunit of 16kDa.
N-terminal amino acid sequences up to 30 amino acid residues suggested that there was essentially no homology with hitherto known lectins. The Agaricus blazei lectin (AGbA) interacted with glycans and glycoproteins containing terminal β-galactose residues, such as asialofetuin, human salivary mucin, lactose-BSA. plant xyloglucan. Lincorice AGP etc . These precipitation reactions and the inhibition studies indicated that AGbA must recognize the β-galactose at the terminal end. AGbA was shown to be a glycoprotein (neutral carbohydrate, 5.2% ; Man : Fuc=4.8 : 1.0), and the specific interaction with α-mannose-binding Crocuss lectin suggested a possible glycopeptide chain with (1,3) α-mannosyl mannose terminals.
