DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, H | ko |
dc.contributor.author | Park, Tae Gwan | ko |
dc.date.accessioned | 2009-11-24T01:38:47Z | - |
dc.date.available | 2009-11-24T01:38:47Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2002-06 | - |
dc.identifier.citation | PHARMACEUTICAL RESEARCH, v.19, no.6, pp.845 - 851 | - |
dc.identifier.issn | 0724-8741 | - |
dc.identifier.uri | http://hdl.handle.net/10203/13173 | - |
dc.description.abstract | Purpose. To isolate mono-PEGylated epidermal growth factor (EGF) isoforms, identify the site of PEGylation, and evaluate the biologic activity of each isoform. Methods. EGF was PEGylated with an NHS-PEG derivative (Mw 3,400). Mono-PEGylated EGF fraction was separated by gel-filtration HPLC and three mono-PEGylated EGF isoforms were purified by RP-HPLC. Tryptic digestion mapping of both EGF and mono-PEGylated EGF isoforms was performed to identify the PEGylation sites using RP-HPLC. The digested fragments were also analyzed by matrix-assisted laser desorption and ionization time of flight (MALDI-TOF) mass spectroscopy for further verification of the three PEG conjugation sites. The biologic activity of positional isoforms was evaluated by a cell proliferation assay and a receptor tyrosine kinase activity assay to determine the effect of PEGylation site on its activity. Results. Mono-PEGylated EGF was composed of three positional isomers. Tryptic digestion mapping and MALDI-TOF analysis permitted the identification of the PEGylated site of the three isoforms at N-terminus, Lysine 28, and Lysine 48. PEG-N-terminus EGF, among the three positional isomers, showed the highest activity in a cell proliferation assay and in a receptor-binding assay. Conclusion. This study demonstrates that biologic activities of mono-PEGylated EGF isomers are highly dependent upon the site of PEGylation in EGF. | - |
dc.description.sponsorship | the Center for Advanced Functional Polymers, KAIST, Korea. | en |
dc.language | English | - |
dc.language.iso | en_US | en |
dc.publisher | KLUWER ACADEMIC/PLENUM PUBL | - |
dc.title | Preparation and characterization of mono-PEGylated epidermal growth factor: Evaluation of in vitro biologic activity | - |
dc.type | Article | - |
dc.identifier.wosid | 000176760300017 | - |
dc.identifier.scopusid | 2-s2.0-003628883 | - |
dc.type.rims | ART | - |
dc.citation.volume | 19 | - |
dc.citation.issue | 6 | - |
dc.citation.beginningpage | 845 | - |
dc.citation.endingpage | 851 | - |
dc.citation.publicationname | PHARMACEUTICAL RESEARCH | - |
dc.identifier.doi | 10.1023/A:1016113117851 | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | Park, Tae Gwan | - |
dc.contributor.nonIdAuthor | Lee, H | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | epidermal growth factor (EGF) | - |
dc.subject.keywordAuthor | polyethylene glycol (PEG) | - |
dc.subject.keywordAuthor | peptide mapping | - |
dc.subject.keywordAuthor | biologic activity | - |
dc.subject.keywordPlus | SITE-DIRECTED MUTAGENESIS | - |
dc.subject.keywordPlus | POLYETHYLENE-GLYCOL | - |
dc.subject.keywordPlus | POSITIONAL ISOMERS | - |
dc.subject.keywordPlus | CONJUGATION | - |
dc.subject.keywordPlus | DELIVERY | - |
dc.subject.keywordPlus | EGF | - |
dc.subject.keywordPlus | STABILITY | - |
dc.subject.keywordPlus | RECEPTOR | - |
dc.subject.keywordPlus | H-1-NMR | - |
dc.subject.keywordPlus | PEPTIDE | - |
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