Purification and characterization of a lectin from the toxic mushroom Amanita pantherina.
A lectin (APL) was isolated from the mushroom Amantia pantherina by means of hydrophobic chromatography on Butyl-Toyopearl, affinity chromatography on bovine submaxillary mucin (BSM)-Toyopearl and gel filtration on Superose 12 HR10/30 using a FPLC system. This lectin is composed of two identical subunits of 22 kDa and the molecular mass of the intact lectin was estimated to be 43 kDa by gel filtration. In hemagglutination inhibition assays, it exhibits sugar-binding specificities towards GlcNAc beta 1-->4Man beta-pNP, Gal beta 1-->4GlcNAc beta 1-->4GlcNAc, and Gal beta 1-->4GlcNAc beta 1-->4GlcNAc beta 1-->4GlcNAc among mono- and oligosaccharides tested. Among glycoproteins tested, BSM and asialo-BSM were the strongest inhibitors.
Zhuang
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Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University, Japan.
Murata
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Usui
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Kawagishi
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Kobayashi
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D000545:Amanita / Q000737:chemistry*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002240:Carbohydrate Sequence; D002846:Chromatography, Affinity / Q000379:methods; D006384:Hemagglutination; D006385:Hemagglutination Inhibition Tests; D006801:Humans; D007526:Isoelectric Point; D037102:Lectins / Q000737:chemistry* / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D017421:Sequence Analysis
D000596:Amino Acids; D037102:Lectins