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.
Kawagishi
H
H
Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University Japan.
Abe
Y
Y
Nagata
T
T
Kimura
A
A
Chiba
S
S
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