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GrainGenes Reference Report: PYC-63-249

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Reference	PYC-63-249
Title	Cys/Gly-rich proteins with a putative single chitin-binding domain from oat (Avena sativa) seeds
Journal	Phytochemistry
Year	2003
Volume	63
Pages	249-255
Author	Li SS Claeson P
Abstract	Summary: Through a reliable and repeatable procedure based on solid-phase extraction techniques, a protein fraction (P fraction) rich in Cys/Gly residues was extracted and captured from oat (Avena sativa L.) seeds. Quantitative amino acid analysis and MS of the P fraction indicated that it contains a series of heterogeneous Cys/Gly-rich proteins with molecular masses of 3.6-4.0 kDa. Preliminary results from bioassays showed that these proteins possess weak to moderate antifungal properties to some fungal strains. From this fraction, a new polypeptide, designated avesin A, was purified and sequenced by Edman degradation. Avesin A consists of 37 amino-acid residues, with 10 glycine residues and eight cysteine residues forming disulfide bridges, and contains a single chitin-binding domain, which indicates that avesin A is a new member of the putative chitin-binding proteins. Avesin A is the first identified hevein-like small protein from cereal grains
Keyword	antifungal [ Show all 34 ]

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