Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1993-10-26
pubmed:abstractText
A high-level production system in Escherichia coli for an alkaline serine protease inhibitor, termed Streptomyces subtilisin inhibitor (SSI), from S. albogriseolus S-3253 was established by replacing the SSI signal sequence with the OmpA signal sequence using the inducible pIN-III-ompA vector. Significant amounts of recombinant SSI, resulting from accurate cleavage of the OmpA signal peptide, were accumulated in the periplasmic space or excreted into the culture medium. The inhibitory activity of the processed protein against subtilisin BPN' was identical with that of authentic SSI. Furthermore, deletion of one of the putative dual terminators (terminator 1) resulted in a 1.9-fold increase in production. This effect on SSI gene expression efficiency was found to be governed mainly at the transcription level.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0175-7598
pubmed:author
pubmed:issnType
Print
pubmed:volume
39
pubmed:geneSymbol
ompA
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
732-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Improved leader and putative terminator sequences for high-level production of Streptomyces subtilisin inhibitor in Escherichia coli.
pubmed:affiliation
Department of Biological Science and Technology, Science University of Tokyo, Chiba, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't