Source:http://linkedlifedata.com/resource/pubmed/id/15044113
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2004-3-26
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pubmed:abstractText |
Non-specific lipid transfer proteins (nsLTPs) are abundant and ubiquitous cystine-rich proteins that are capable, in vitro, of binding lipids and hydrophobic molecules. In view to probe the lipid binding properties of the wheat nsLTP1, mutant variants may represent a powerful tool. To this end, a synthetic gene, encoding a mature wheat nsLTP1 polypeptide, was designed to ensure high level expression in Escherichia coli. The bacterial expression host strain, a translational fusion strategy, and convenient cleavage and purification procedures were optimized to produce in standard fermentation conditions, a significant amount (15 mg/L final yield), of a soluble and correctly folded recombinant nsLTP1. This highly amenable expression system is helpful in order to investigate structure-activity relationships of plant nsLTP.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cystine,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/lipid transfer proteins, plant
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
316
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1202-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15044113-Antigens, Plant,
pubmed-meshheading:15044113-Carrier Proteins,
pubmed-meshheading:15044113-Cystine,
pubmed-meshheading:15044113-Escherichia coli,
pubmed-meshheading:15044113-Gene Expression Regulation, Bacterial,
pubmed-meshheading:15044113-Genetic Enhancement,
pubmed-meshheading:15044113-Mutagenesis, Site-Directed,
pubmed-meshheading:15044113-Plant Proteins,
pubmed-meshheading:15044113-Protein Engineering,
pubmed-meshheading:15044113-Recombinant Proteins,
pubmed-meshheading:15044113-Triticum
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pubmed:year |
2004
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pubmed:articleTitle |
A bacterial expression system revisited for the recombinant production of cystine-rich plant lipid transfer proteins.
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pubmed:affiliation |
Unité de Recherche sur les Protéines Végétales et leurs Interactions, INRA, Rue de la Géraudière 44316 Nantes Cedex 3, France. elmorjan@nantes.inra.fr
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't,
Evaluation Studies
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