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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2003-5-28
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pubmed:abstractText |
We compared the functional properties of two insect members of the phospholipid hydroperoxide glutathione peroxidases (PHGPx) family, VLP1, a major component of virus-like particles from the hymenopteran endoparasitoid Venturia canescens and its closest Drosophila relative, one of the putative PHGPx-proteins predicted from the Berkeley Drosophila genome sequence project. Recombinant Drosophila PHGPx shows enzymatic activity towards a number of PHGPx substrates, while the recombinant PHGPx-like domain of VLP1 lacks a functionally relevant cysteine and enzyme activity. A possible function of a non-enzymatic extracellular PHGPx-like protein is discussed.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0022-1910
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
49
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12770011-Amino Acid Sequence,
pubmed-meshheading:12770011-Animals,
pubmed-meshheading:12770011-Base Sequence,
pubmed-meshheading:12770011-Blotting, Northern,
pubmed-meshheading:12770011-DNA Primers,
pubmed-meshheading:12770011-Drosophila,
pubmed-meshheading:12770011-Genome,
pubmed-meshheading:12770011-Glutathione Peroxidase,
pubmed-meshheading:12770011-Humans,
pubmed-meshheading:12770011-Hymenoptera,
pubmed-meshheading:12770011-Molecular Sequence Data,
pubmed-meshheading:12770011-Open Reading Frames,
pubmed-meshheading:12770011-Phylogeny,
pubmed-meshheading:12770011-Recombinant Proteins,
pubmed-meshheading:12770011-Sequence Alignment,
pubmed-meshheading:12770011-Sequence Homology, Amino Acid,
pubmed-meshheading:12770011-Substrate Specificity,
pubmed-meshheading:12770011-Transcription, Genetic
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pubmed:year |
2003
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pubmed:articleTitle |
Possible function of two insect phospholipid-hydroperoxide glutathione peroxidases.
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pubmed:affiliation |
Department of Applied and Molecular Ecology, Waite Campus, Adelaide University, Glen Osmond, SA 5064, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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