《Lyase Activities of Heterologous CpcS and CpcT for Phycocyanin Holoβsubunit from Arthrospira platensis in Escherichia coli》.pdfVIP

下载本文档

4
0
约4.33万字
约 6页
2015-10-01 发布于浙江
举报
版权申诉

《Lyase Activities of Heterologous CpcS and CpcT for Phycocyanin Holoβsubunit from Arthrospira platensis in Escherichia coli》.pdf

1、原创力文档（book118）网站文档一经付费（服务费），不意味着购买了该文档的版权，仅供个人/单位学习、研究之用，不得用于商业用途，未经授权，严禁复制、发行、汇编、翻译或者网络传播等，侵权必究。。
2、本站所有内容均由合作方或网友上传，本站不对文档的完整性、权威性及其观点立场正确性做任何保证或承诺！文档内容仅供研究参考，付费前请自行鉴别。如您付费，意味着您自己接受本站规则且自行承担风险，本站不退款、不进行额外附加服务；查看《如何避免下载的几个坑》。如果您已付费下载过本站文档，您可以点击这里二次下载。
3、如文档侵犯商业秘密、侵犯著作权、侵犯人身权等，请点击“版权申诉”（推荐），也可以打举报电话：400-050-0827(电话支持时间：9:00-18:30)。
4、该文档为VIP文档，如果想要下载，成为VIP会员后，下载免费。
5、成为VIP后，下载本文档将扣除1次下载权益。下载后，不支持退款、换文档。如有疑问请联系我们。
6、成为VIP后，您将拥有八大权益，权益包括：VIP文档下载权益、阅读免打扰、文档格式转换、高级专利检索、专属身份标志、高级客服、多端互通、版权登记。
7、VIP文档为合作方或网友上传，每下载1次，网站将根据用户上传文档的质量评分、类型等，对文档贡献者给予高额补贴、流量扶持。如果你也想贡献VIP文档。上传文档

J. Ocean Univ. China (Oceanic and Coastal Sea Research) DOI 10.1007/s11802-014-2161-0 ISSN 1672-5182, 2014 13 (3): 497-502 /xbywb/ E-mail:xbywb@ Lyase Activities of Heterologous CpcS and CpcT for Phycocyanin Holo-β-subunit from Arthrospira platensis in Escherichia coli YI Junjie1), XU Di1), *, ZANG Xiaonan1), YUAN Dingyang2), ZHAO Bingran2), TANG Li2), TAN Yanning2), and ZHANG Xuecheng1) 1) Key Laboratory of Marine Genetics and Breeding (Ocean University of China), Ministry of Education, Qingdao 266003, P. R. China 2) State Key Laboratory of Hybrid Rice, Hunan Hybrid Rice Research Center, Changsha 410125, P. R. China (Received September 27, 2012; revised December 5, 2012; accepted October 30, 2013) © Ocean University of China, Science Press and Spring-Verlag Berlin Heidelberg 2014 Abstract Arthrospira platensis is an economically important cyanobacterium; and it has been used widely in food and pharmaceu- tical industries. The phycocyanin (PC) from A. platensis is extremely valuable in medicine and molecular biology due to its anti- oxidation and anti-tumoring activity and applicability as fluorescence protein tag. In present study, two recombinant plasmids, one contained the phycocyanobilin (PCB)-producing genes (hox1 and pcyA ) while the other contained the phycobiliprotein gene (cpcB) and the lyase gene (either cpcS/U or cpcT), were constructed and synchronically transferred into E. coli in order to test the the activi- ties of relevant lyases for catalysing PCB addition to CpcB during synthesizing fluorescent PC holo-β-subunit (β-PC) of A. platensis . As was evidenced by the fluorescence emitted at a peak specific for PC, CpcB was successfully synthesized in E. coli, to which co-expressed PCBs attached though at a relatively low efficiency. The results showed that the attachment of PCBs to CpcB were carried out mainly by co-expressed CpcS/U but CpcB also showed some autocatalytic activity. Currently, no CpcT