Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/18953
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dc.contributor.authorPozidis, C.en
dc.contributor.authorLammertyn, E.en
dc.contributor.authorPolitou, A. S.en
dc.contributor.authorAnne, J.en
dc.contributor.authorTsiftsoglou, A. S.en
dc.contributor.authorSianidis, G.en
dc.contributor.authorEconomou, A.en
dc.date.accessioned2015-11-24T18:55:55Z-
dc.date.available2015-11-24T18:55:55Z-
dc.identifier.issn0006-3592-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/18953-
dc.rightsDefault Licence-
dc.subjectBioreactorsen
dc.subjectCell Culture Techniques/*methodsen
dc.subjectCulture Media/pharmacologyen
dc.subjectFeasibility Studiesen
dc.subjectFermentationen
dc.subjectGlucose/pharmacologyen
dc.subjectPilot Projectsen
dc.subjectPolymers/metabolismen
dc.subjectQuality Controlen
dc.subjectRecombinant Proteins/biosynthesis/secretionen
dc.subjectStreptomyces/drug effects/*metabolismen
dc.subjectTumor Necrosis Factor-alpha/biosynthesis/chemistry/isolation &en
dc.subjectpurification/*secretionen
dc.titleProtein secretion biotechnology using Streptomyces lividans: large-scale production of functional trimeric tumor necrosis factor alphaen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/11460252-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1002/1097-0290(20010320)72:6<611::AID-BIT1026>3.0.CO;2-0/asset/26_ftp.pdf?v=1&t=h0dhin0k&s=79311a00ec2b3431d643e7afd06abf6432fe8bbd-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2001-
heal.abstractWe evaluated the feasibility of large-scale production of biopharmaceuticals expressed as heterologous polypeptides from the Gram-positive bacterium Streptomyces lividans. As a model protein we used murine tumor necrosis factor alpha (mTNFalpha). mTNFalpha fused C-terminally to the secretory signal peptide of the subtilisin-inhibitor protein from Streptomyces venezuelae. Under appropriate fermentation conditions, significant amounts of mature mTNFalpha (80-120 mg/L) can be recovered from spent growth media. Efficient downstream processing allowing rapid purification of mTNFalpha from culture supernatants was developed. Importantly, the protein is recovered from the spent growth medium in its native trimeric state as judged by biophysical analysis. Further, mTNFalpha secreted by S. lividans is significantly more active in an in vitro apoptosis tissue culture assay than a corresponding polypeptide produced in Escherichia coli. This pilot study provides the first validation of S. lividans protein secretion as an alternative bioprocess for large-scale production of oligomeric proteins of potential therapeutic value.en
heal.journalNameBiotechnol Bioengen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ

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