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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2016.8
- 수록면
- 903 - 912 (10page)
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초록· 키워드
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Hagfish which belongs to the chordate contact cyclostomata, is important phylogenetic relationship between vertebrate and invertebrate. Cathepsins of the cysteine protease family have traditionally been thought to play a major role in intracellular protein degradation and turnover in lysosomes.
In this study, Catepsin L was cloned from Inshore hagfish (Eptatretus burgeri), the cDNA encoding ORF of the Eptatretus burgeri Cathepsin L (EbCtL) is 978 bp. The cDNA encoding proEbCtL was expressed in Escherichia coli strain BL21(DE3) using the pGEX-4T-1 expression vector system. The recombinant proEbCtL protein was overexpressed as a approximately 55 kDa fusion protein. The overproduced soluble GST-fusion protein was then applied to glutathione-Sepharose 4B column chromatography; the sample harboring the fusion protein evidenced a high degree of purity when analyzed via SDS-PAGE and Western blot analysis. Its activity was quantied by cleaving the synthetic peptide Z-FR-AMC, Z-LLE-AMC, and Suc-AAF-AMC, and the optimal pH for the protease activity was 8, 9.5, and 9, respectively.
In this study, Catepsin L was cloned from Inshore hagfish (Eptatretus burgeri), the cDNA encoding ORF of the Eptatretus burgeri Cathepsin L (EbCtL) is 978 bp. The cDNA encoding proEbCtL was expressed in Escherichia coli strain BL21(DE3) using the pGEX-4T-1 expression vector system. The recombinant proEbCtL protein was overexpressed as a approximately 55 kDa fusion protein. The overproduced soluble GST-fusion protein was then applied to glutathione-Sepharose 4B column chromatography; the sample harboring the fusion protein evidenced a high degree of purity when analyzed via SDS-PAGE and Western blot analysis. Its activity was quantied by cleaving the synthetic peptide Z-FR-AMC, Z-LLE-AMC, and Suc-AAF-AMC, and the optimal pH for the protease activity was 8, 9.5, and 9, respectively.
목차
Abstract
Ⅰ. Introduction
Ⅱ. Materials and methods
Ⅲ. Results and discussion
References
참고문헌 (25)
참고문헌 신청
[학술지(정기간행물)] - Barrett, A. J. / 1981 / cathepsin B, cathepsin H, and cathepsin L / Methods in Enzymology 80 : 535 ~ 561
[단행본] - Barrett A. J. / 1998 / Hand book of Proteolytic Enzymes / Academic Press : 258 ~
[학술지(정기간행물)] - Dacks, J. B. / 2008 / Phylogenetic and primary sequence characterization of cathepsin B cysteine proteases from the oxymonad flagellate monocercomonoides / Journal of Eukaryotic Microbiology 55 (1) : 9 ~ 17
[학술지(정기간행물)] - Duncan, E. M / 2008 / Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation / Cell 135 (2) : 284 ~ 294
[학술지(정기간행물)] - Fonović, M. / 2014 / Cysteine cathepsins and their potential in clinical therapy and biomarker discovery / PROTEOMICS-Clinical Applications 8 (5-6) : 416 ~ 426
[단행본] - Barrett A. J. / 1998 / Hand book of Proteolytic Enzymes / Academic Press : 258 ~
[학술지(정기간행물)] - Dacks, J. B. / 2008 / Phylogenetic and primary sequence characterization of cathepsin B cysteine proteases from the oxymonad flagellate monocercomonoides / Journal of Eukaryotic Microbiology 55 (1) : 9 ~ 17
[학술지(정기간행물)] - Duncan, E. M / 2008 / Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation / Cell 135 (2) : 284 ~ 294
[학술지(정기간행물)] - Fonović, M. / 2014 / Cysteine cathepsins and their potential in clinical therapy and biomarker discovery / PROTEOMICS-Clinical Applications 8 (5-6) : 416 ~ 426
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UCI(KEPA) : I410-ECN-0101-2017-454-000980811