A lectin from the mushroom Pholiota aurivella.
A lectin was isolated from the fruiting bodies of Pholiota aurivella by preparative PAGE and named PAA (Pholiota aurivella agglutinin). PAA was a polymeric protein of more than several hundred kDa consisting of 18-kDa subunits. The amino acids were sequenced from the N-terminus of the lectin; they were YSVTTPNSVKGGTNQG. PAA agglutinated human erythrocytes regardless of blood type equally and Pronase treatment of erythrocytes increased the sensitivity to agglutination by the lectin. In a hemaggluting inhibition assay, none of the mono-and oligosaccharides used affected agglutination by the lectin. Among glycoproteins, asialofetuin was the best inhibitor. This is first isolated and characterized lectin from the family Strophariaceae.
Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University Japan.
H
H
Kawagishi
Y
Y
Abe
T
T
Nagata
A
A
Kimura
S
S
Chiba
D000595:Amino Acid Sequence; D001487:Basidiomycota / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D004903:Erythrocyte Aggregation / Q000187:drug effects; D005656:Fungal Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D006023:Glycoproteins / Q000494:pharmacology; D006388:Hemagglutinins / Q000302:isolation & purification; D006801:Humans; D037102:Lectins / Q000302:isolation & purification*; D008969:Molecular Sequence Data
D005656:Fungal Proteins; D006023:Glycoproteins; D006388:Hemagglutinins; D037102:Lectins