Interactions between U(VI) and bovine serum albumin
文献类型：期刊论文
| ; | |
| 作者 | Yang, Y; Feng YX(冯一潇) ; Feng, YX; Wang, YF; Wang, L; Shi, WQ; Wang L(王琳); Shi WQ(石伟群)
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| 刊名 | JOURNAL OF RADIOANALYTICAL AND NUCLEAR CHEMISTRY
 ; JOURNAL OF RADIOANALYTICAL AND NUCLEAR CHEMISTRY
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| 出版日期 | 2013 ; 2013 |
| 卷号 | 298期号:2页码:903-908 |
| 关键词 | Uranium BSA Secondary structure FT-IR/ATR Uranium BSA Secondary structure FT-IR/ATR |
| ISSN号 | 0236-5731 |
| DOI | 10.1007/s10967-013-2487-x |
| 英文摘要 | Interest in bio-toxicology of uranium resulting from its radioactive heavy metal property has been growing enormously in recent years. The interactions between uranium(VI) [U(VI)] and bovine serum albumin (BSA) at physiological pH were studied by spectroscopic methods. Fuorescence results revealed the formation of BSA-U(VI) complex, the binding constants as well as the number of binding sites were determined. In particular, the effects of U(VI) binding on the secondary structures of BSA were examined by means of Fourier transformation infrared spectroscopy equipped with attenuated total reflection (FT-IR/ATR). It was found that the alpha-helix component of BSA decreased gradually with increasing concentration of U(VI). In contrast, the beta-sheets, turns, and random coil structures all increased correspondingly. Our work would shed light on the possible interaction mechanism between U(VI) and proteins in aqueous solutions.; Interest in bio-toxicology of uranium resulting from its radioactive heavy metal property has been growing enormously in recent years. The interactions between uranium(VI) [U(VI)] and bovine serum albumin (BSA) at physiological pH were studied by spectroscopic methods. Fuorescence results revealed the formation of BSA-U(VI) complex, the binding constants as well as the number of binding sites were determined. In particular, the effects of U(VI) binding on the secondary structures of BSA were examined by means of Fourier transformation infrared spectroscopy equipped with attenuated total reflection (FT-IR/ATR). It was found that the alpha-helix component of BSA decreased gradually with increasing concentration of U(VI). In contrast, the beta-sheets, turns, and random coil structures all increased correspondingly. Our work would shed light on the possible interaction mechanism between U(VI) and proteins in aqueous solutions. |
| 学科主题 | Chemistry; Nuclear Science & Technology ; Chemistry; Nuclear Science & Technology |
| 收录类别 | SCI |
| 电子版国际标准刊号 | 1588-2780 |
| 语种 | 英语 |
| WOS记录号 | WOS:000325624300021 ; WOS:000325624300021 |
| 公开日期 | 2016-05-03 |
| 源URL | [http://ir.ihep.ac.cn/handle/311005/224079]  |
| 专题 | 高能物理研究所_多学科研究中心 |
| 推荐引用方式 GB/T 7714 | Yang, Y,Feng YX,Feng, YX,et al. Interactions between U(VI) and bovine serum albumin, Interactions between U(VI) and bovine serum albumin[J]. JOURNAL OF RADIOANALYTICAL AND NUCLEAR CHEMISTRY, JOURNAL OF RADIOANALYTICAL AND NUCLEAR CHEMISTRY,2013, 2013,298, 298(2):903-908, 903-908. |
| APA | Yang, Y.,冯一潇.,Feng, YX.,Wang, YF.,Wang, L.,...&石伟群.(2013).Interactions between U(VI) and bovine serum albumin.JOURNAL OF RADIOANALYTICAL AND NUCLEAR CHEMISTRY,298(2),903-908. |
| MLA | Yang, Y,et al."Interactions between U(VI) and bovine serum albumin".JOURNAL OF RADIOANALYTICAL AND NUCLEAR CHEMISTRY 298.2(2013):903-908. |
入库方式： OAI收割
来源：高能物理研究所
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