中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
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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