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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
1998-10-22
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pubmed:abstractText |
We have produced single-chain antibody fragments (scFv) in Saccharomyces cerevisiae at levels up to 20 mg/L in shake flask culture by a combination of expression level tuning and overexpression of folding assistants. Overexpression of the chaperone BiP or protein disulfide isomerase (PDI) increases secretion titers 2-8 fold for five scFvs. The increases occur for scFv expression levels ranging from low copy to ER-saturating overexpression. The disulfide isomerase activity of PDI, rather than its chaperone activity, is responsible for the secretion increases. A synergistic increase in scFv production occurs upon cooverexpression of BiP and PDI.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Variable Region,
http://linkedlifedata.com/resource/pubmed/chemical/McPC603 antibody,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Disulfide-Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/molecular chaperone GRP78
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1087-0156
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
773-7
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9702778-Amino Acid Substitution,
pubmed-meshheading:9702778-Antibodies,
pubmed-meshheading:9702778-Blotting, Western,
pubmed-meshheading:9702778-Carrier Proteins,
pubmed-meshheading:9702778-Catalysis,
pubmed-meshheading:9702778-Chromatography, Affinity,
pubmed-meshheading:9702778-Cysteine,
pubmed-meshheading:9702778-Endoplasmic Reticulum,
pubmed-meshheading:9702778-Gene Dosage,
pubmed-meshheading:9702778-Gene Expression Regulation,
pubmed-meshheading:9702778-Genetic Vectors,
pubmed-meshheading:9702778-Heat-Shock Proteins,
pubmed-meshheading:9702778-Immunoglobulin Fragments,
pubmed-meshheading:9702778-Immunoglobulin Variable Region,
pubmed-meshheading:9702778-Molecular Chaperones,
pubmed-meshheading:9702778-Protein Disulfide-Isomerases,
pubmed-meshheading:9702778-Protein Folding,
pubmed-meshheading:9702778-Recombinant Proteins,
pubmed-meshheading:9702778-Saccharomyces cerevisiae
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pubmed:year |
1998
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pubmed:articleTitle |
Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments.
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pubmed:affiliation |
Department of Chemical Engineering, University of Illinois, Urbana 61801, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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