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
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Research Support, Non-U.S. Gov't
MeSH terms
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Agaricales / chemistry*
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Amino Acid Sequence
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Antifungal Agents / chemistry
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Antifungal Agents / isolation & purification
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Antifungal Agents / pharmacology*
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Biological Assay
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Complex Mixtures / chemistry
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Complex Mixtures / isolation & purification
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Complex Mixtures / pharmacology*
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Electrophoresis, Polyacrylamide Gel
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Flammulina / drug effects*
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Flammulina / growth & development
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Fruiting Bodies, Fungal / chemistry
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Fungal Proteins / chemistry
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Fungal Proteins / isolation & purification
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Fungal Proteins / pharmacology*
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Molecular Weight
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Peptide Mapping
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Ribonuclease H / chemistry
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Sequence Homology, Amino Acid
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Substances
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Antifungal Agents
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Complex Mixtures
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Fungal Proteins
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HM-af protein, Hypsizygus marmoreus
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Ribonuclease H