Gene cloning and functional analysis of glycosaminoglycan-degrading enzyme chondroitin AC lyase from Flavobacterium columnare G(4)
文献类型:期刊论文
作者 | Xie, HX; Nie, P; Chang, MX; Liu, Y; Yao, WJ |
刊名 | ARCHIVES OF MICROBIOLOGY |
出版日期 | 2005-10-01 |
卷号 | 184期号:1页码:49-55 |
ISSN号 | 0302-8933 |
关键词 | chondroitin AC lyase gene cloning recombinant protein lytic activity Flavobacterium columnare G4 |
通讯作者 | Nie, P, Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Hubei, Peoples R China |
中文摘要 | The chondroitin AC lyase gene, cslA, was cloned for the first time from the fish bacterial pathogen F. columnare G(4). From the first transcription initiation site, the cslA extends 2620 nucleotides to the end of the 3' region. The open reading frame of cslA transcript has 2286 nucleotides encoding 762 amino acids with a 16 residues long signal peptide at the N-terminus. The gene, cslA was then successfully expressed in Escherichia coli and recombinant chondroitin AC lyase, rChonAC was purified, with its lytic activity analyzed. Zymography analysis copolymerized with chondroitin sulphate revealed the lytic activity of rChonAC and also the crude native ChonAC isolated from periplamic space of cultured F. columnare G(4). The low level of lytic activity observed in crude native ChonAC may be due possibly to the low level of expression of this gene in the cultured condition. The expression and the role of this virulence factor is of interest for further research on the pathogenesis of F. columnare. |
英文摘要 | The chondroitin AC lyase gene, cslA, was cloned for the first time from the fish bacterial pathogen F. columnare G(4). From the first transcription initiation site, the cslA extends 2620 nucleotides to the end of the 3' region. The open reading frame of cslA transcript has 2286 nucleotides encoding 762 amino acids with a 16 residues long signal peptide at the N-terminus. The gene, cslA was then successfully expressed in Escherichia coli and recombinant chondroitin AC lyase, rChonAC was purified, with its lytic activity analyzed. Zymography analysis copolymerized with chondroitin sulphate revealed the lytic activity of rChonAC and also the crude native ChonAC isolated from periplamic space of cultured F. columnare G(4). The low level of lytic activity observed in crude native ChonAC may be due possibly to the low level of expression of this gene in the cultured condition. The expression and the role of this virulence factor is of interest for further research on the pathogenesis of F. columnare. |
学科主题 | Microbiology |
WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
类目[WOS] | Microbiology |
研究领域[WOS] | Microbiology |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000233041400007 |
公开日期 | 2010-10-13 |
源URL | [http://ir.ihb.ac.cn/handle/152342/9112] |
专题 | 水生生物研究所_中科院水生所知识产出(2009年前)_期刊论文 |
作者单位 | 1.Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Hubei, Peoples R China 2.Chinese Acad Sci, Inst Hydrobiol, Lab Fish Dis, Wuhan 430072, Hubei, Peoples R China |
推荐引用方式 GB/T 7714 | Xie, HX,Nie, P,Chang, MX,et al. Gene cloning and functional analysis of glycosaminoglycan-degrading enzyme chondroitin AC lyase from Flavobacterium columnare G(4)[J]. ARCHIVES OF MICROBIOLOGY,2005,184(1):49-55. |
APA | Xie, HX,Nie, P,Chang, MX,Liu, Y,&Yao, WJ.(2005).Gene cloning and functional analysis of glycosaminoglycan-degrading enzyme chondroitin AC lyase from Flavobacterium columnare G(4).ARCHIVES OF MICROBIOLOGY,184(1),49-55. |
MLA | Xie, HX,et al."Gene cloning and functional analysis of glycosaminoglycan-degrading enzyme chondroitin AC lyase from Flavobacterium columnare G(4)".ARCHIVES OF MICROBIOLOGY 184.1(2005):49-55. |
入库方式: OAI收割
来源:水生生物研究所
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