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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1989-6-8
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pubmed:abstractText |
We have made deletions in a human interleukin 1 beta cDNA cloned in a yeast vector capable of directing the expression and secretion of foreign protein. Deletions at either the 5' or 3' end of the cDNA result in a dramatic drop in yield of protein. An investigation of some possible causes points to instability of the truncated peptides as a major factor contributing to low yield. The results suggest that correct folding of mature interleukin 1 into a protease resistant form requires almost the entire polypeptide.
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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:issn |
0269-2139
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
433-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2469082-Base Sequence,
pubmed-meshheading:2469082-Chromosome Deletion,
pubmed-meshheading:2469082-Gene Expression Regulation,
pubmed-meshheading:2469082-Genetic Vectors,
pubmed-meshheading:2469082-Interleukin-1,
pubmed-meshheading:2469082-Mutation,
pubmed-meshheading:2469082-Nucleic Acid Hybridization,
pubmed-meshheading:2469082-RNA,
pubmed-meshheading:2469082-Saccharomyces cerevisiae
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pubmed:articleTitle |
Differential stability of human interleukin 1 beta fragments expressed in yeast.
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pubmed:affiliation |
Sclavo Research Center, Siena, Italy.
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pubmed:publicationType |
Journal Article,
Comparative Study
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