A novel lectin from the wild mushroom Polyporus adusta

Biochem Biophys Res Commun. 2003 Aug 1;307(3):535-9. doi: 10.1016/s0006-291x(03)01230-0.

Abstract

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.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Division / drug effects
  • Cells, Cultured
  • Fungal Proteins / chemistry
  • Fungal Proteins / isolation & purification*
  • Fungal Proteins / pharmacology*
  • Hemagglutinins / chemistry
  • Hemagglutinins / isolation & purification
  • Hemagglutinins / pharmacology
  • Lectins / chemistry
  • Lectins / isolation & purification*
  • Lectins / pharmacology*
  • Mice
  • Molecular Sequence Data
  • Polyporaceae / chemistry*
  • Sequence Alignment

Substances

  • Fungal Proteins
  • Hemagglutinins
  • Lectins