DC Field | Value | Language |
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dc.contributor.author | Hwang, DS | - |
dc.contributor.author | Gim Young Soo | - |
dc.contributor.author | CHA, HYUNG JOON | - |
dc.date.accessioned | 2016-04-01T02:44:50Z | - |
dc.date.available | 2016-04-01T02:44:50Z | - |
dc.date.created | 2010-11-04 | - |
dc.date.issued | 2005-05 | - |
dc.identifier.issn | 8756-7938 | - |
dc.identifier.other | 2005-OAK-0000021803 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/25693 | - |
dc.description.abstract | Mussel adhesive proteins, including the 20-plus variants of foot protein type 3 (fp-3), have been suggested as potential environmentally friendly adhesives for use in aqueous conditions and in medicine. Here we report the novel production of a recombinant Mytilus galloprovincialis foot protein type 3 variant A (Mgfp-3A) fused with a hexahistidine affinity ligand in Escherichia coli and its ∼ 99% purification with affinity chromatography. Recombinant Mgfp-3A showed a superior purification yield and better apparent solubility in 5% acetic acid (prerequisites for large-scale production and practical use) compared to those of the previously reported recombinant M. galloprovincialis foot protein type 5 (Mgfp-5). The adsorption abilities and adhesion forces of purified recombinant Mgfp-3A were compared with those of Cell-Tak (a commercial mussel extract adhesive) and recombinant Mgfp-5 using quartz crystal microbalance analysis and modified atomic force microscopy, respectively. These assays showed that the adhesive ability of recombinant Mgfp-3A was comparable to that of Cell-Tak but lower than that of recombinant Mgfp-5. Collectively, these results indicate that recombinant Mgfp-3A may be useful as a commercial bioadhesive or an adhesive ingredient in medical or underwater environments. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | Wiley | - |
dc.relation.isPartOf | BIOTECHNOLOGY PROGRESS | - |
dc.subject | ATOMIC-FORCE MICROSCOPE | - |
dc.subject | MYTILUS-EDULIS-L | - |
dc.subject | PLAQUE PROTEIN | - |
dc.subject | FAMILY | - |
dc.title | expression of functional recombinant mussel adhesive protein type 3A in Escherichia coli | - |
dc.type | Article | - |
dc.contributor.college | 해양대학원 | - |
dc.identifier.doi | 10.1021/BP050014E | - |
dc.author.google | Hwang, DS | - |
dc.author.google | Gim, Y | - |
dc.author.google | Cha, HJ | - |
dc.relation.volume | 21 | - |
dc.relation.issue | 3 | - |
dc.relation.startpage | 965 | - |
dc.relation.lastpage | 970 | - |
dc.contributor.id | 10167197 | - |
dc.relation.journal | BIOTECHNOLOGY PROGRESS | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCI | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | BIOTECHNOLOGY PROGRESS, v.21, no.3, pp.965 - 970 | - |
dc.identifier.wosid | 000229605400044 | - |
dc.date.tcdate | 2019-02-01 | - |
dc.citation.endPage | 970 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 965 | - |
dc.citation.title | BIOTECHNOLOGY PROGRESS | - |
dc.citation.volume | 21 | - |
dc.contributor.affiliatedAuthor | Hwang, DS | - |
dc.contributor.affiliatedAuthor | CHA, HYUNG JOON | - |
dc.identifier.scopusid | 2-s2.0-20144366711 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 53 | - |
dc.description.scptc | 42 | * |
dc.date.scptcdate | 2018-05-121 | * |
dc.type.docType | Article | - |
dc.subject.keywordPlus | ATOMIC-FORCE MICROSCOPE | - |
dc.subject.keywordPlus | MYTILUS-EDULIS-L | - |
dc.subject.keywordPlus | PLAQUE PROTEIN | - |
dc.subject.keywordPlus | FAMILY | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.relation.journalWebOfScienceCategory | Food Science & Technology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
dc.relation.journalResearchArea | Food Science & Technology | - |
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