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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1995-3-15
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pubmed:abstractText |
An artificial synthetic gene coding for human eIF-4E was cloned into an expression vector and direct expression was attempted in Escherichia coli [BL21(DE3) strain] under the control of T7 promoter. The active gene product which was induced in high yield (ca. 4 mg/100 ml) by isopropyl-beta-D-thiogalactopyranoside was purified to homogeneity by a two-step chromatographic procedure with a good yield (ca. 74%), and was confirmed to be recombinant human eIF-4E by amino acid composition and sequence analyses, isoelectric focusing, and absorption spectral measurements. The identity of three-dimensional structures between the recombinant and native human eIF-4Es was confirmed by CD and fluorescence measurements.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-924X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
116
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
687-93
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:7852292-Amino Acid Sequence,
pubmed-meshheading:7852292-Base Sequence,
pubmed-meshheading:7852292-Chemistry, Physical,
pubmed-meshheading:7852292-Cloning, Molecular,
pubmed-meshheading:7852292-Escherichia coli,
pubmed-meshheading:7852292-Eukaryotic Initiation Factor-4E,
pubmed-meshheading:7852292-Gene Expression Regulation, Bacterial,
pubmed-meshheading:7852292-Genes, Synthetic,
pubmed-meshheading:7852292-Humans,
pubmed-meshheading:7852292-Molecular Sequence Data,
pubmed-meshheading:7852292-Peptide Initiation Factors,
pubmed-meshheading:7852292-Physicochemical Phenomena,
pubmed-meshheading:7852292-Plasmids,
pubmed-meshheading:7852292-Recombinant Proteins
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pubmed:year |
1994
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pubmed:articleTitle |
Direct expression of a synthetic gene in Escherichia coli: purification and physicochemical properties of human initiation factor 4E.
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pubmed:affiliation |
Department of Physical Chemistry, Osaka University of Pharmaceutical Sciences.
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pubmed:publicationType |
Journal Article
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