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rdf:type |
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lifeskim:mentions |
|
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pubmed:issue |
5
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pubmed:dateCreated |
2001-10-23
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|
pubmed:abstractText |
A basic heme-peroxidase (WP1) was purified to homogeneity from wheat (Triticum aestivum) kernels. The protein was not glycosylated and exhibited a molecular mass of 36 kDa and a pI of 8.0. The N-terminal amino acid sequence revealed a very high similarity with a wheat flour peroxidase allergen associated with baker's asthma. WPI showed indole-3-acetic acid oxidase activity in the presence of Mn2+ and phenolic cofactors. Antifungal assays performed in vitro towards phytopathogenic fungi indicated that WP1 was active in inhibiting germ tube elongation. This first report on antifungal properties of a heme-peroxidase gives experimental support to the idea that peroxidases play a defensive role against invading pathogens.
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pubmed:language |
eng
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pubmed:journal |
|
|
pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0031-9422
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pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:volume |
58
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
743-50
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11672739-Amino Acid Sequence,
pubmed-meshheading:11672739-Antifungal Agents,
pubmed-meshheading:11672739-Botrytis,
pubmed-meshheading:11672739-Fusarium,
pubmed-meshheading:11672739-Manganese,
pubmed-meshheading:11672739-Molecular Sequence Data,
pubmed-meshheading:11672739-Peroxidase,
pubmed-meshheading:11672739-Peroxidases,
pubmed-meshheading:11672739-Seeds,
pubmed-meshheading:11672739-Sequence Homology,
pubmed-meshheading:11672739-Trichoderma,
pubmed-meshheading:11672739-Triticum
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pubmed:year |
2001
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|
pubmed:articleTitle |
A basic peroxidase from wheat kernel with antifungal activity.
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|
pubmed:affiliation |
Dipartimento di Agrobiologia e Agrochimica Università della Tuscia, Via S. Camillo De Lellis, I-01100, Viterbo, Italy. caruso@unitus.it
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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