Heterologous expression and purification of recombinant allophycocyanin in marine Streptomyces sp isolate M097
文献类型：期刊论文
| 作者 | Hou, YH; Qin, S; Li, YX ; Li, FC; Xia, HZ; Zhao, FQ
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| 刊名 | WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY
 |
| 出版日期 | 2006-05-01 |
| 卷号 | 22期号:5页码:525-529 |
| 关键词 | Allophycocyanin Conjugal Transfer Heterologous Expression Marine Purification Streptomyces |
| ISSN号 | 0959-3993 |
| DOI | 10.1007/s11274-005-9067-3 |
| 文献子类 | Article |
| 英文摘要 | Allophycocyanin is one of the most important marine active peptides. Previous studies suggested that recombinant allophycocyanin (rAPC) could remarkably inhibit the S-180 carcinoma in mice, indicating its potential pharmaceutical uses. Based on intergeneric conjugal transfer, heterologous expression of rAPC was first achieved in marine Streptomyces sp. isolate M097 through inserting the apc gene into the thiostrepton-induced vector pIJ8600. The transformation frequency for this system was approximately 10(-4) exconjugants/recipient. In the transformed Streptomyces sp. isolate M097, the yield of purified rAPC could amount to about 38 mg/l using a simple purification protocol, and HPLC analysis showed that the purity of the protein reached about 91.5%. In vitro activity tests also revealed that the purified rAPC had effective scavenging abilities on superoxide and hydroxyl radicals. This would widen the usefulness of the marine Streptomyces as a host to express the rAPC and to offer industrial strain for the production of rAPC.; Allophycocyanin is one of the most important marine active peptides. Previous studies suggested that recombinant allophycocyanin (rAPC) could remarkably inhibit the S-180 carcinoma in mice, indicating its potential pharmaceutical uses. Based on intergeneric conjugal transfer, heterologous expression of rAPC was first achieved in marine Streptomyces sp. isolate M097 through inserting the apc gene into the thiostrepton-induced vector pIJ8600. The transformation frequency for this system was approximately 10(-4) exconjugants/recipient. In the transformed Streptomyces sp. isolate M097, the yield of purified rAPC could amount to about 38 mg/l using a simple purification protocol, and HPLC analysis showed that the purity of the protein reached about 91.5%. In vitro activity tests also revealed that the purified rAPC had effective scavenging abilities on superoxide and hydroxyl radicals. This would widen the usefulness of the marine Streptomyces as a host to express the rAPC and to offer industrial strain for the production of rAPC. |
| 学科主题 | Biotechnology & Applied Microbiology |
| URL标识 | 查看原文 |
| 语种 | 英语 |
| WOS记录号 | WOS:000237468600018 |
| 公开日期 | 2010-12-24 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/5837]  |
| 专题 | 海洋研究所_实验海洋生物学重点实验室 |
| 作者单位 | 1.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China 3.Shenyang Pharmaceut Univ, Dept Biopharmaceut, Shenyang 110016, Peoples R China |
| 推荐引用方式 GB/T 7714 | Hou, YH,Qin, S,Li, YX,et al. Heterologous expression and purification of recombinant allophycocyanin in marine Streptomyces sp isolate M097[J]. WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY,2006,22(5):525-529. |
| APA | Hou, YH,Qin, S,Li, YX,Li, FC,Xia, HZ,&Zhao, FQ.(2006).Heterologous expression and purification of recombinant allophycocyanin in marine Streptomyces sp isolate M097.WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY,22(5),525-529. |
| MLA | Hou, YH,et al."Heterologous expression and purification of recombinant allophycocyanin in marine Streptomyces sp isolate M097".WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY 22.5(2006):525-529. |
入库方式： OAI收割
来源：海洋研究所
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