Expression and purification of the anticomplementary peptide Sh-CRIT-ed1 (formerly Sh-TOR-ed1) as a tetramultimer in Escherichia coli
DC Field | Value | Language |
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dc.contributor.author | Oh, Kwang-Seok | - |
dc.contributor.author | Na, Do-Kyun | - |
dc.contributor.author | Kweon, Mee-Hyang | - |
dc.contributor.author | Sung, Ha-Chin | - |
dc.date.available | 2020-11-20T06:40:47Z | - |
dc.date.issued | 2003-02 | - |
dc.identifier.issn | 1046-5928 | - |
dc.identifier.issn | 1096-0279 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/43530 | - |
dc.description.abstract | Many complement inhibitors found in plants and other organisms have been recognized as an antiinflammatory drug. Sh-CRIT-ed1 is a complement inhibitory peptide, present on the Schistosoma parasite surface. In the present study, we expressed chemically synthesized oligonucleotides encoding Sh-CRIT-ed1 with an additional hexahistidine codon at the C-terminus and purified in Escherichia coli BL21. The cloned gene, which was multimerized four times in pBlue-script II KS (+) at the isoschizomer sites (BamHI, Bg/II), was named Sh4, and expressed in E. coli BL21 harboring pGEX-KG. The fusion protein (GST-Sh4) was purified with high yield successively by affinity chromatographies of glutathione-Sepharose 4B and Ni-NTA-agarose. Recombinant Sh-CRIT-ed1 I was obtained readily by thrombin digestion and CNBr cleavage of GST-Sh4, and the yield was 9.03 mg from 1-liter culture of E. coli BL21 harboring pGEX-Sh4. The recombinant Sh-CRIT-ed1 showed strong anticomplementary activity (IC50 = 6.02 muM) by complement haemolysis assay. (C) 2002 Elsevier Science (USA). All rights reserved. | - |
dc.format.extent | 8 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.title | Expression and purification of the anticomplementary peptide Sh-CRIT-ed1 (formerly Sh-TOR-ed1) as a tetramultimer in Escherichia coli | - |
dc.type | Article | - |
dc.identifier.doi | 10.1016/S1046-5928(02)00598-3 | - |
dc.identifier.bibliographicCitation | PROTEIN EXPRESSION AND PURIFICATION, v.27, no.2, pp 202 - 209 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.wosid | 000181405600002 | - |
dc.identifier.scopusid | 2-s2.0-0037296217 | - |
dc.citation.endPage | 209 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 202 | - |
dc.citation.title | PROTEIN EXPRESSION AND PURIFICATION | - |
dc.citation.volume | 27 | - |
dc.type.docType | Article | - |
dc.publisher.location | 미국 | - |
dc.subject.keywordAuthor | Sh-CRIT | - |
dc.subject.keywordAuthor | anticomplementary peptide | - |
dc.subject.keywordAuthor | expression | - |
dc.subject.keywordAuthor | repetitive artificial peptide and Escherichia coli | - |
dc.subject.keywordPlus | COMPLEMENT-SYSTEM | - |
dc.subject.keywordPlus | TANDEM REPEATS | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | INHIBITORS | - |
dc.subject.keywordPlus | CLEAVAGE | - |
dc.subject.keywordPlus | RECEPTOR | - |
dc.subject.keywordPlus | STRATEGY | - |
dc.subject.keywordPlus | MUCIN | - |
dc.subject.keywordPlus | TOR | - |
dc.subject.keywordPlus | C2 | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
dc.relation.journalWebOfScienceCategory | Biochemical Research Methods | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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