An antifungal protein from the culinary-medicinal beech mushroom, Hypsizygus marmoreus (Peck) Bigel. (Agaricomycetideae)

Int J Med Mushrooms. 2011;13(1):27-31. doi: 10.1615/intjmedmushr.v13.i1.40.

Abstract

An antifungal protein (HM-af) was purified from the culinary-medicinal mushroom Hypsizygus marmoreus. The results of sodium dodecyl sulfate polyacrylamide gel electrophoresis and matrix-assisted laser desorption ionization time-of-flight mass spectrometry of HM-af indicated that its molecular mass was 9.5 kDa. The N-terminal amino acid sequence of HM-af showed homology to ribonuclease H from Clostridium thermocellum. HM-af showed the antifungal activity against Flammulina velutipes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agaricales / chemistry*
  • Amino Acid Sequence
  • Antifungal Agents / chemistry
  • Antifungal Agents / isolation & purification
  • Antifungal Agents / pharmacology*
  • Biological Assay
  • Complex Mixtures / chemistry
  • Complex Mixtures / isolation & purification
  • Complex Mixtures / pharmacology*
  • Electrophoresis, Polyacrylamide Gel
  • Flammulina / drug effects*
  • Flammulina / growth & development
  • Fruiting Bodies, Fungal / chemistry
  • Fungal Proteins / chemistry
  • Fungal Proteins / isolation & purification
  • Fungal Proteins / pharmacology*
  • Molecular Weight
  • Peptide Mapping
  • Ribonuclease H / chemistry
  • Sequence Homology, Amino Acid
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Substances

  • Antifungal Agents
  • Complex Mixtures
  • Fungal Proteins
  • HM-af protein, Hypsizygus marmoreus
  • Ribonuclease H