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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0002245,
umls-concept:C0004595,
umls-concept:C0015980,
umls-concept:C0025914,
umls-concept:C0026809,
umls-concept:C0036536,
umls-concept:C0036537,
umls-concept:C0086022,
umls-concept:C0205177,
umls-concept:C0205460,
umls-concept:C0220781,
umls-concept:C0442335,
umls-concept:C1705099,
umls-concept:C1883254
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pubmed:issue |
1
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pubmed:dateCreated |
1985-8-15
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M11006,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M11007,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M11008,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M11009,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M11010,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M11011,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M11013,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M11014
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pubmed:abstractText |
Mouse interferon-beta (IFN-beta) cDNA, whose signal sequence had been removed by BAL 31 digestion, was introduced into a Bacillus subtilis secretion vector constructed by using the promoter and signal sequence of the B. subtilis alpha-amylase gene. The resultant chimeric plasmids were transferred into B. subtilis 207-25. Four kanamycin-resistant transformants were selected by both colony hybridization and a new immunoblot method for secretory proteins. They secrete the proteins which cross-react with sheep anti-mouse IFN-beta serum into the culture medium. One of them expressed a high IFN-beta activity as assayed by the L cell and vesicular stomatitis virus system, while the other three showed weak or little IFN activities. Based on our previous study [Ohmura et al., Nucl. Acids Res. 12 (1984) 5307-5319], it was suggested that the secreted IFN molecules are hybrid proteins in which the NH2-terminal region consists of part of the alpha-amylase signal peptide. Nucleotide sequence analysis revealed that plasmid pTUB502, which expressed high IFN activity, is joined to the mouse IFN-beta gene from the codon position 6 of its mature protein. The other three plasmids, pTUB506, pTUB509, and pTUB519, contain the mouse IFN-beta gene from the codon positions 3, 1, and -5, respectively. The NH2-terminal region of the mouse IFN-beta seems to be closely related to its biological activity.
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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 |
0378-1119
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
34
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-8
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:3924734-Animals,
pubmed-meshheading:3924734-Bacillus subtilis,
pubmed-meshheading:3924734-Bacterial Proteins,
pubmed-meshheading:3924734-Base Sequence,
pubmed-meshheading:3924734-Cloning, Molecular,
pubmed-meshheading:3924734-Genetic Vectors,
pubmed-meshheading:3924734-Interferon Type I,
pubmed-meshheading:3924734-Mice,
pubmed-meshheading:3924734-Plasmids,
pubmed-meshheading:3924734-Protein Processing, Post-Translational,
pubmed-meshheading:3924734-alpha-Amylases
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pubmed:year |
1985
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pubmed:articleTitle |
Synthesis and secretion of biologically active mouse interferon-beta using a Bacillus subtilis alpha-amylase secretion vector.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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