Purification of recombinant wheat cytochrome P450 monooxygenase expressed in yeast and its properties
文献类型：期刊论文
| 作者 | Xiang, WS; Wang, XJ; Ren, TR; Ci, SQ |
| 刊名 | PROTEIN EXPRESSION AND PURIFICATION
 |
| 出版日期 | 2006 |
| 卷号 | 45期号:1页码:54-59 |
| ISSN号 | 1046-5928 |
| 关键词 | wheat cytochrome P450 purification FPLC properties herbicide |
| 其他题名 | Protein Expr. Purif. |
| 中文摘要 | To investigate the properties of wheat cytochrome P450 and the characteristics of herbicide metabolism by cytochrome P450 in vitro, deeply understand the mechanisms of herbicide selectivity, recombinant wheat cytochrome P450 monooxygenase (CYP71Cv1) heterologously expressed in yeast was purified by DE-52 cellulose chromatography and fast protein liquid chromatography (FPLC) with Mono-Q column. The degree of purification was 1366-fold. The specific activity of purified cytochrome P450 reached to 512 nmol min(-1) mg(-1) protein with herbicide chlorsulfuron as substrate. The purified cytochrome P450 exhibited one band in sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, and the molecular mass was 52.5 kDa. Kinetic parameter was determined in vitro. The K-m values for chlorsulfuron and triasulfuron were 57 (+/-15) and 38 (+/-16) mu M, respectively; and V-max for chlorsulfuron and triasulfuron were 4.1 (+/-0.7) and 2.7 (+/-0.5) nmol min(-1) mg(-1) protein in vitro, respectively. (C) 2005 Elsevier Inc. All rights reserved. |
| 英文摘要 | To investigate the properties of wheat cytochrome P450 and the characteristics of herbicide metabolism by cytochrome P450 in vitro, deeply understand the mechanisms of herbicide selectivity, recombinant wheat cytochrome P450 monooxygenase (CYP71Cv1) heterologously expressed in yeast was purified by DE-52 cellulose chromatography and fast protein liquid chromatography (FPLC) with Mono-Q column. The degree of purification was 1366-fold. The specific activity of purified cytochrome P450 reached to 512 nmol min(-1) mg(-1) protein with herbicide chlorsulfuron as substrate. The purified cytochrome P450 exhibited one band in sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, and the molecular mass was 52.5 kDa. Kinetic parameter was determined in vitro. The K-m values for chlorsulfuron and triasulfuron were 57 (+/-15) and 38 (+/-16) mu M, respectively; and V-max for chlorsulfuron and triasulfuron were 4.1 (+/-0.7) and 2.7 (+/-0.5) nmol min(-1) mg(-1) protein in vitro, respectively. (C) 2005 Elsevier Inc. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemical Research Methods ; Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology |
| 关键词[WOS] | PLANT CYTOCHROME-P450 ; HERBICIDE METABOLISM ; MOLECULAR-CLONING ; CYP76B1 ; CHLORSULFURON ; BIOSYNTHESIS ; LINURON ; PROTEIN ; TOBACCO ; ENZYME |
| 收录类别 | SCI |
| 原文出处 | |
| 语种 | 英语 |
| WOS记录号 | WOS:000234521100007 |
| 公开日期 | 2013-10-24 |
| 版本 | 出版稿 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/4058]  |
| 专题 | 过程工程研究所_研究所（批量导入） |
| 作者单位 | 1.Chinese Acad Sci, Inst Proc Engn, State Key Lab Biochem Engn, Beijing 100080, Peoples R China 2.NE Agr Univ, Res Ctr Life Sci & Biotechnol, Harbin 150030, Peoples R China |
| 推荐引用方式 GB/T 7714 | Xiang, WS,Wang, XJ,Ren, TR,et al. Purification of recombinant wheat cytochrome P450 monooxygenase expressed in yeast and its properties[J]. PROTEIN EXPRESSION AND PURIFICATION,2006,45(1):54-59. |
| APA | Xiang, WS,Wang, XJ,Ren, TR,&Ci, SQ.(2006).Purification of recombinant wheat cytochrome P450 monooxygenase expressed in yeast and its properties.PROTEIN EXPRESSION AND PURIFICATION,45(1),54-59. |
| MLA | Xiang, WS,et al."Purification of recombinant wheat cytochrome P450 monooxygenase expressed in yeast and its properties".PROTEIN EXPRESSION AND PURIFICATION 45.1(2006):54-59. |
入库方式： OAI收割
来源：过程工程研究所
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