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Hyeon-Kyeong JO(조현경),Jun-Young CHAE(채준영),Hyung-Ho LEE(이형호) 한국수산해양교육학회 2018 水産海洋敎育硏究 Vol.30 No.5
Inshore hagfish (Eptatretus burgeri) belongs to chordate and cyclostomata, so it is considered to be an important organism for the study of embryology and biological evolution. Protein kinase C (PKC) performs a wide range of biological functions regarding proliferation, apoptosis, differentiation, motility, and inflammation with cellular signal transduction. In this study, PKC beta isoforms, a member of the conventional class, were cloned. As a result, EbPKCβI and EbPKCβII showed the same sequence in conserved regions (C1, C2, C3, and C4 domain), but not in the C-terminal called the V5 domain. The ORFs of EbPKCβI and EbPKCβII were 2,007 bp and 2,004 bp, respectively. In the analysis of tissue specific expression patterns by qPCR, EbPKCβI was remarkably highly expressed in the root of the tongue and the spinal cord, while EbPKCβII was highly expressed in the gill, liver, and gut. The EbPKC βI and EbPKCβII expressed in E. coli revealed PKC activity according to both qualitative analysis and quantitative analysis.
Jin-Hyeon JANG(장진현),So-Hee SON(손소희),Hyeon-Kyeong JO(조현경),Joon-Ki CHUNG(정준기),Hyung-Ho LEE(이형호) 한국수산해양교육학회 2016 水産海洋敎育硏究 Vol.28 No.4
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.