Purification and partial characterization of L-fucose-specific lectin from fruit bodies of Peziza badia Merat.
An L-fucose-specific lectin from fruit bodies of the ascomycete Peziza badia Merat, was purified by affinity chromatography on agarose-coupled human ovariomucin (serotype H). This lectin binds L-fucose but is not specific to erythrocytes of blood group O(I), similarly to the lectin from Aleuria aurantia ascomycete. Unlike L-fucose-specific plant lectins, the lectin from P. badia binds with human thyroglobulin and mannofucogalactans of aphyllophoric fungi; this suggests that the lectin interacts with L-fucose located inside the polysaccharide chain of the glycoconjugates. Thus, the immunochemical properties of the lectins from P. badia and A. aurantia are similar.
Antonyuk
V A
VA
Division of Regulatory Cell Systems, Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Lvov, Ukraine.
D001203:Ascomycota / Q000737:chemistry*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005643:Fucose / Q000737:chemistry*; D006801:Humans; D037102:Lectins / Q000737:chemistry / Q000302:isolation & purification*; D009077:Mucins / Q000737:chemistry
D037102:Lectins; D009077:Mucins; D005643:Fucose