Improved non-chromatographic purification of a recombinant protein by cationic elastin-like polypeptides
DC Field | Value | Language |
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dc.contributor.author | Lim, Dong Woo | - |
dc.contributor.author | Trabbic-Carlson, Kimberly | - |
dc.contributor.author | MacKay, J. Andrew | - |
dc.contributor.author | Chilkoti, Ashutosh | - |
dc.date.accessioned | 2021-06-23T19:41:24Z | - |
dc.date.available | 2021-06-23T19:41:24Z | - |
dc.date.created | 2021-01-21 | - |
dc.date.issued | 2007-05 | - |
dc.identifier.issn | 1525-7797 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/43762 | - |
dc.description.abstract | This paper reports an improvement in the purification of thioredoxin (Trx) expressed from E. coli by inverse transition cycling (ITC) using cationic elastin-like polypeptides (ELPs). Two ELP libraries having 2% and 5% lysine residues and molecular weights ranging from 4 to 61.1 kDa showed greater salt sensitivity in their inverse transition behavior than purely aliphatic ELPs. Expression yield of Trx-ELP fusions was an unpredictable function of guest residue composition, but reducing the molecular weight of the ELP tag generally increased Trx yield. A cationic 4.3 kDa ELP is the shortest ELP used to purify any protein by ITC to date. A 15.9 kDa ELP with a guest residue composition of K:V:F of 1:7:1 was found to be the optimal cationic tag to purify Trx, as it provided 50% greater Trx yield and only required one-fifth the added NaCl for purification of Trx as compared to previously used aliphatic ELP tags. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.title | Improved non-chromatographic purification of a recombinant protein by cationic elastin-like polypeptides | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Lim, Dong Woo | - |
dc.identifier.doi | 10.1021/bm060849t | - |
dc.identifier.scopusid | 2-s2.0-34249903605 | - |
dc.identifier.wosid | 000246413600008 | - |
dc.identifier.bibliographicCitation | BIOMACROMOLECULES, v.8, no.5, pp.1417 - 1424 | - |
dc.relation.isPartOf | BIOMACROMOLECULES | - |
dc.citation.title | BIOMACROMOLECULES | - |
dc.citation.volume | 8 | - |
dc.citation.number | 5 | - |
dc.citation.startPage | 1417 | - |
dc.citation.endPage | 1424 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.relation.journalResearchArea | Polymer Science | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Organic | - |
dc.relation.journalWebOfScienceCategory | Polymer Science | - |
dc.subject.keywordPlus | INVERSE TEMPERATURE TRANSITION | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | TRIGGERED PURIFICATION | - |
dc.subject.keywordPlus | CHAIN-LENGTH | - |
dc.subject.keywordPlus | FUSION | - |
dc.subject.keywordPlus | TAGS | - |
dc.subject.keywordPlus | IMMOBILIZATION | - |
dc.subject.keywordPlus | BIOSEPARATION | - |
dc.subject.keywordPlus | IMMUNOASSAY | - |
dc.subject.keywordPlus | BIOPOLYMERS | - |
dc.identifier.url | https://pubs.acs.org/doi/10.1021/bm060849t | - |
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