Simple Purification of the Human Antimicrobial Peptide Dermcidin (MDCD-1L) by Intein-Mediated Expression in E-coli
DC Field | Value | Language |
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dc.contributor.author | Hong, Inpyo | - |
dc.contributor.author | Kim, Yong-Seok | - |
dc.contributor.author | Choi, Shin-Geon | - |
dc.date.accessioned | 2022-12-20T19:08:30Z | - |
dc.date.available | 2022-12-20T19:08:30Z | - |
dc.date.created | 2022-08-27 | - |
dc.date.issued | 2010-02 | - |
dc.identifier.issn | 1017-7825 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/175488 | - |
dc.description.abstract | Among human antimicrobial peptides (hAMPs), DCD-1L has a broad spectrum of antimicrobial activity over a wide pH range and in high salt concentrations. It offers a promising alternative to conventional antibiotics. The 458-bp-long dermcidin cDNA was amplified by PCR using a human fetal cDNA library as a template. The 147-bp fragment of the MDCD-1L gene encoding an additional methionine residue was subcloned into the pTYB11 vector. Recombinant MDCD-1L was expressed as an intein fusion protein in E coli, and then purified by affinity chromatography using chitin beads. A small peptide with a molecular mass of about 5 kDa was detected by tricine gel electrophoresis. The recombinant MDCD-1L peptide was purified from the gel and its amino acid sequence was determined by nanoLC-ESI-MS/MS analysis. The initiating amino acid, methionine, remained attached to the N-terminal region of recombinant MDCD-1L. Purified MDCD-1L showed antimicrobial activity against a Micrococcus luteus test strain. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY | - |
dc.title | Simple Purification of the Human Antimicrobial Peptide Dermcidin (MDCD-1L) by Intein-Mediated Expression in E-coli | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, Yong-Seok | - |
dc.identifier.doi | 10.4014/jmb.0907.07029 | - |
dc.identifier.scopusid | 2-s2.0-77649214723 | - |
dc.identifier.wosid | 000275103400017 | - |
dc.identifier.bibliographicCitation | JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.20, no.2, pp.350 - 355 | - |
dc.relation.isPartOf | JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY | - |
dc.citation.title | JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY | - |
dc.citation.volume | 20 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 350 | - |
dc.citation.endPage | 355 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.identifier.kciid | ART001420526 | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
dc.relation.journalResearchArea | Microbiology | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.relation.journalWebOfScienceCategory | Microbiology | - |
dc.subject.keywordPlus | ECCRINE SWEAT | - |
dc.subject.keywordPlus | MEMBRANES | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordPlus | GLANDS | - |
dc.subject.keywordPlus | CHARGE | - |
dc.subject.keywordPlus | CELLS | - |
dc.subject.keywordAuthor | Antimicrobial peptides | - |
dc.subject.keywordAuthor | DCD-1L | - |
dc.subject.keywordAuthor | dermcidin | - |
dc.subject.keywordAuthor | intein | - |
dc.subject.keywordAuthor | protein expression | - |
dc.identifier.url | https://www.jmb.or.kr/journal/view.html?doi=10.4014/jmb.0907.07029 | - |
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