Purification and characterization of a lectin from the mushroom Mycoleptodonoides aitchisonii.
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.
Kawagishi
H
H
Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University, Japan. achkawa@agr.shizuoka.ac.jp
Takagi
J
J
Taira
T
T
Murata
T
T
Usui
T
T
D000363:Agaricales / Q000737:chemistry*; D000596:Amino Acids / Q000032:analysis; D002853:Chromatography, Liquid / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D037102:Lectins / Q000737:chemistry / Q000302:isolation & purification*; D020349:Surface Plasmon Resonance
D000596:Amino Acids; D037102:Lectins