DC Field | Value | Language |
---|---|---|
dc.contributor.author | Chung, BH | ko |
dc.contributor.author | Choi, YJ | ko |
dc.contributor.author | Yoon, SH | ko |
dc.contributor.author | Lee, SangYup | ko |
dc.contributor.author | Lee, YI | ko |
dc.date.accessioned | 2010-12-02T06:00:36Z | - |
dc.date.available | 2010-12-02T06:00:36Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2000-02 | - |
dc.identifier.citation | JOURNAL OF INDUSTRIAL MICROBIOLOGY BIOTECHNOLOGY, v.24, no.2, pp.94 - 99 | - |
dc.identifier.issn | 1367-5435 | - |
dc.identifier.uri | http://hdl.handle.net/10203/20642 | - |
dc.description.abstract | Fed-batch cultures were carried out to overproduce human insulin-like growth factor I (IGF-I) in Escherichia coli. The effects of carbon sources (glucose or glycerol) and induction time on cell growth and IGF-I production were investigated in more detail. Glycerol was a better carbon source than glucose for IGF-I production in fed-batch culture. Induction at the mid-exponential phase with glycerol as a carbon source in the pH-stat fed-batch culture was optimal for IGF-l production. Under this condition, 2.8 g L-1 of fusion IGF-I was produced as inclusion bodies. We have also developed downstream processing for preparative scale purification of IGF-I from the fusion protein produced by the fed-batch culture using glycerol as a carbon source. After the fusion protein expressed was solubilized in 8 M urea and cleaved with hydroxylamine, the released IGF-I was purified by cation exchange chromatography, refolding and preparative scale reverse phase HPLC (rp-HPLC) to give recombinant IGF-I of >98% purity. The biological activities of the purified IGF-I were measured and found to be identical to those of commercial IGF-I. | - |
dc.description.sponsorship | Part of this work was presented at the APBioCheC'97 in Beijing. This work was supported by the Ministry of Science and Technology. | en |
dc.language | English | - |
dc.language.iso | en_US | en |
dc.publisher | STOCKTON PRESS | - |
dc.title | Process development for production Of recombinant human insulin-like growth factor-I in Escherichia coli | - |
dc.type | Article | - |
dc.identifier.wosid | 000086864400003 | - |
dc.identifier.scopusid | 2-s2.0-0034015457 | - |
dc.type.rims | ART | - |
dc.citation.volume | 24 | - |
dc.citation.issue | 2 | - |
dc.citation.beginningpage | 94 | - |
dc.citation.endingpage | 99 | - |
dc.citation.publicationname | JOURNAL OF INDUSTRIAL MICROBIOLOGY BIOTECHNOLOGY | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | Lee, SangYup | - |
dc.contributor.nonIdAuthor | Chung, BH | - |
dc.contributor.nonIdAuthor | Choi, YJ | - |
dc.contributor.nonIdAuthor | Yoon, SH | - |
dc.contributor.nonIdAuthor | Lee, YI | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | insulin-like growth factor I (IGF-I) | - |
dc.subject.keywordAuthor | fed-batch culture | - |
dc.subject.keywordAuthor | downstream processing | - |
dc.subject.keywordAuthor | Escherichia coli | - |
dc.subject.keywordPlus | SOMATOMEDIN-C | - |
dc.subject.keywordPlus | IGF-I | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | GENE | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | YEAST | - |
dc.subject.keywordPlus | SECRETION | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | CULTURE | - |
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