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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	[ Hide all but 1 of 34 ] antifungal antifungal properties avena avena sativa avesin a bridges cereal grains chitin binding cysteine cysteine residues degradation disulfide bridge domain extraction fraction glycine grains gramineae isolation and identification latex mass member molecular mass oat polypeptide protein protein fraction psi-blast quantitative sequence series smart tool tree hevea brasiliensis

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