rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
1984-6-13
|
pubmed:abstractText |
The stability of mRNA for the delta-lysin of Staphylococcus aureus was determined by measuring the residual lysin synthesis after inhibition of DNA-dependent RNA polymerase activity with rifampin. At the late logarithmic-early stationary phase of growth the delta-lysin mRNA was very stable, with a half-life of ca. 20 min. Total cellular RNA was extracted from S. aureus and translated with a modified Escherichia coli S-30 system; delta-lysin was identified amongst the translation products by immunoprecipitation and immunoabsorption. The delta-lysin synthesized in vitro was of a size similar to mature delta-lysin and did not require a signal sequence for secretion from the cell.
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pubmed:commentsCorrections |
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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 |
May
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pubmed:issn |
0019-9567
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
44
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
434-8
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:6201445-Bacterial Proteins,
pubmed-meshheading:6201445-Cell-Free System,
pubmed-meshheading:6201445-DNA-Directed RNA Polymerases,
pubmed-meshheading:6201445-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6201445-Escherichia coli,
pubmed-meshheading:6201445-Hemolysin Proteins,
pubmed-meshheading:6201445-Kinetics,
pubmed-meshheading:6201445-Protein Biosynthesis,
pubmed-meshheading:6201445-RNA, Bacterial,
pubmed-meshheading:6201445-RNA, Messenger,
pubmed-meshheading:6201445-Rifampin,
pubmed-meshheading:6201445-Staphylococcus aureus
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pubmed:year |
1984
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pubmed:articleTitle |
In vitro synthesis of the delta-lysin of Staphylococcus aureus.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|