Isolation of a novel N-acetylglucosamine-specific lectin from fresh sclerotia of the edible mushroom Pleurotus tuber-regium

Protein Expr Purif. 2003 Jun;29(2):156-60. doi: 10.1016/s1046-5928(03)00059-7.

Abstract

An N-acetylglucosamine-binding lectin with a molecular mass of 32kDa was isolated from fresh sclerotia of the edible mushroom Pleurotus tuber-regium. Its N-terminal sequence exhibited some similarity to that of Agaricus bisporus lectin. The isolation procedure was simple, involving (NH(4))(2)SO(4) precipitation, ion exchange chromatography on DEAE-cellulose, affinity chromatography on N-acetyl-D-glucosamine-agarose, and gel filtration by fast protein liquid chromatography on Superdex 75. The lectin exhibited hemagglutinating activity toward trypsinized rabbit erythrocytes but not toward untrypsinized rabbit erythrocytes.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / metabolism*
  • Amino Acid Sequence
  • Animals
  • Chromatography, Affinity
  • Chromatography, Gel
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics
  • Fungal Proteins / isolation & purification*
  • Fungal Proteins / metabolism*
  • Hemagglutination Tests
  • Lectins / chemistry
  • Lectins / genetics
  • Lectins / isolation & purification*
  • Lectins / metabolism*
  • Molecular Sequence Data
  • Pleurotus / chemistry*
  • Rabbits
  • Sequence Analysis, Protein

Substances

  • Agaricus lectins
  • Fungal Proteins
  • Lectins
  • Acetylglucosamine