Recombinant expression of human cathelicidin (hCAP18/LL-37) in Pichia pastoris
DC Field | Value | Language |
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dc.contributor.author | Hong, In-Pyo | - |
dc.contributor.author | Lee, Sung-Jae | - |
dc.contributor.author | Kim, Yong-Seok | - |
dc.contributor.author | Choi, Shin-Geon | - |
dc.date.accessioned | 2022-12-21T09:35:24Z | - |
dc.date.available | 2022-12-21T09:35:24Z | - |
dc.date.created | 2022-08-26 | - |
dc.date.issued | 2007-01 | - |
dc.identifier.issn | 0141-5492 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/180591 | - |
dc.description.abstract | The constitutive expression of human cathelicidin LL-37 antimicrobial peptide was achieved using the methylotrophic yeast, Pichia pastoris. An LL-37 cDNA clone was amplified by PCR using human fetal cDNA library as template. The 111 bp fragment encoding mature LL-37 gene was subcloned into pGAPZ-E, an episomal form of the pGAPZB vector incorporating PARS1. It was then transformed into the P. pastoris X-33 strain for intracellular expression. A small peptide with a molecular mass of about 5 kDa was detected by 17% peptide-PAGE analysis. The recombinant LL-37 peptide was purified from the gel and its amino acid sequence was determined by LC-ESI-MS/MS analysis. The initiating amino acid, methionine, was still attached to the N-terminal region of recombinant LL-37. LL-37 crude extract from P. pastoris showed an antimicrobial activity against Micrococcus luteus as the test strain. The successful expression of human LL-37 indicates that the system may be applicable to the expression of other human defensins without resorting to fusion protein constructions. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | SPRINGER | - |
dc.title | Recombinant expression of human cathelicidin (hCAP18/LL-37) in Pichia pastoris | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, Yong-Seok | - |
dc.identifier.doi | 10.1007/s10529-006-9202-8 | - |
dc.identifier.scopusid | 2-s2.0-33845637789 | - |
dc.identifier.wosid | 000242700800009 | - |
dc.identifier.bibliographicCitation | BIOTECHNOLOGY LETTERS, v.29, no.1, pp.73 - 78 | - |
dc.relation.isPartOf | BIOTECHNOLOGY LETTERS | - |
dc.citation.title | BIOTECHNOLOGY LETTERS | - |
dc.citation.volume | 29 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 73 | - |
dc.citation.endPage | 78 | - |
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 | Biotechnology & Applied Microbiology | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.subject.keywordPlus | ANTIMICROBIAL PEPTIDE LL-37 | - |
dc.subject.keywordPlus | HIGH-LEVEL EXPRESSION | - |
dc.subject.keywordPlus | DEFENSINS | - |
dc.subject.keywordPlus | GENE | - |
dc.subject.keywordAuthor | cathelicidin | - |
dc.subject.keywordAuthor | LL-37 | - |
dc.subject.keywordAuthor | heterologous expression | - |
dc.subject.keywordAuthor | Pichia pastoris | - |
dc.identifier.url | https://link.springer.com/article/10.1007/s10529-006-9202-8 | - |
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