Purification and characterization of a lectin from the mushroom Mycoleptodonoides aitchisonii

¹Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University, Japan. achkawa@agr.shizuoka.ac.jp

|February 24, 2001

Abstract:

A lectin was isolated from the mushroom Mycoleptodonoides aitchisonii by means of 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 four identical 16 kDa subunits and the molecular mass of the intact lectin was estimated to be 64 kDa by gel filtration. In a hemagglutination inhibition assay, it exhibited strong sugar-binding specificity towards asialo-BSM among the mono- or oligo-saccharides and glycoproteins tested. The binding specificity of the lectin was also examined by surface plasmon resonance analysis.

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Purification and characterization of a lectin from the mushroom Mycoleptodonoides aitchisonii

Abstract:

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