Abstract
A novel antifungal peptide, with a molecular mass of 8 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and in gel filtration on Superdex 75 and designated cucurmoschin, was isolated from the seeds of the black pumpkin. The peptide was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel. Cucurmoschin inhibited mycelial growth in the fungi Botrytis cinerea, Fusarium oxysporum and Mycosphaerella oxysporum. It inhibited translation in a cell-free rabbit reticulocyte lysate system with an IC50 of 1.2 microM. The N-terminal sequence of cucurmoschin was rich in arginine, glutamate and glycine residues.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Antifungal Agents / analysis*
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Antifungal Agents / isolation & purification
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Antifungal Agents / pharmacology
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Arginine / analysis
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Botrytis / drug effects
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Cell-Free System
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Chromatography, Affinity
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Chromatography, Gel
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Chromatography, Ion Exchange
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Cucurbita / chemistry*
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Defensins / analysis*
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Defensins / isolation & purification
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Defensins / pharmacology
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Electrophoresis, Polyacrylamide Gel
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Fungi / drug effects
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Fusarium / drug effects
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Glutamic Acid / analysis
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Glycine / analysis
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Inhibitory Concentration 50
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Molecular Sequence Data
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Molecular Weight
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Plant Proteins / analysis*
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Plant Proteins / isolation & purification
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Plant Proteins / pharmacology
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Protein Biosynthesis / drug effects
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Rabbits
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Reticulocytes / metabolism
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Seeds / chemistry*
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Triazines / chemistry
Substances
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Antifungal Agents
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Defensins
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Plant Proteins
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Triazines
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cucurmoschin protein, Cucurbita moschata
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Glutamic Acid
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Cibacron Blue F 3GA
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Arginine
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Glycine