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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1992-5-21
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pubmed:abstractText |
An efficient Escherichia coli system for the production of a variant form of the cytotoxic protein alpha-sarcin (delta Ala 1) has been constructed. cDNA encoded alpha-sarcin lacking N-terminal alanine was ligated with the bla signal peptide sequence (the signal sequence of E. coli beta-lactamase localizes the protein in the periplasm) and was inserted into an inducible bacterial expression vector pKTN2-2. When the plasmid introduced into E. coli was expressed in the presence of IPTG, the recombinant product accumulated in the periplasmic space. The product was purified by Affi-Gel Blue followed by Bio-Rex 70 column chromatography. Recombinant alpha-sarcin (delta Ala 1) displayed the properties similar to those of authentic alpha-sarcin isolated from Aspergillus giganteus with respect to its molecular mass and enzymatic activity in ribosomal inactivation. The amount of alpha-sarcin variant produced in the system was estimated to be 1.2 mg/l of culture.
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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 |
Mar
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
1130
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
182-8
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pubmed:dateRevised |
2006-5-1
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pubmed:meshHeading |
pubmed-meshheading:1562594-Amino Acid Sequence,
pubmed-meshheading:1562594-Base Sequence,
pubmed-meshheading:1562594-Blotting, Western,
pubmed-meshheading:1562594-Cloning, Molecular,
pubmed-meshheading:1562594-DNA,
pubmed-meshheading:1562594-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1562594-Endoribonucleases,
pubmed-meshheading:1562594-Escherichia coli,
pubmed-meshheading:1562594-Fungal Proteins,
pubmed-meshheading:1562594-Gene Expression,
pubmed-meshheading:1562594-Genetic Vectors,
pubmed-meshheading:1562594-Molecular Sequence Data,
pubmed-meshheading:1562594-Plasmids,
pubmed-meshheading:1562594-Protein Synthesis Inhibitors,
pubmed-meshheading:1562594-Recombinant Proteins
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pubmed:year |
1992
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pubmed:articleTitle |
An efficient expression system for a variant form of the cytotoxic protein alpha-sarcin in Escherichia coli.
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pubmed:affiliation |
Department of Nutritional Chemistry, School of Medicine, University of Tokushima, Japan.
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pubmed:publicationType |
Journal Article
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