A novel lectin from the wild mushroom Polyporus adusta.
A lectin with antiproliferative activity toward tumor cell lines and mitogenic activity toward splenocytes was isolated from the mushroom Polyporus adusta. The lectin was composed of two identical subunits each with a molecular weight of 12 kDa. It was adsorbed on both DEAE-cellulose and Q-Sepharose and unadsorbed on CM-Sepharose. The hemagglutinating activity of the lectin was inhibited by turanose and by a large variety of other carbohydrates. It was adversely affected in the presence of NaOH or HCl at a concentration of 7.5mM and above, and when the ambient temperature was raised above 70 degrees C. All divalent and trivalent metallic chlorides tested at 1.25-10mM including CaCl(2), MgCl(2), ZnCl(2), MnCl(2), and AlCl(3), did not alter the hemagglutinating activity of the lectin. FeCl(3) at 10mM caused the hemagglutinating activity to increase by 100%, but it did not change the lectin activity when tested at lower concentrations up to 5mM.
Wang
Hexiang
H
Department of Microbiology, College of Biological Science, China Agricultural University, Beijing, China.
Ng
Tzi Bun
TB
Liu
Qinghong
Q
D000595:Amino Acid Sequence; D000818:Animals; D002455:Cell Division / Q000187:drug effects; D002478:Cells, Cultured; D005656:Fungal Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*; D006388:Hemagglutinins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D037102:Lectins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*; D051379:Mice; D008969:Molecular Sequence Data; D011124:Polyporaceae / Q000737:chemistry*; D016415:Sequence Alignment
D005656:Fungal Proteins; D006388:Hemagglutinins; D037102:Lectins