Investigation of the effects of temperature and ions on the interaction between ECG and BSA by the fluorescence quenching method
The effects of temperature and common ions on binding (-)-epicatechin gallate (ECG) to bovine serum albumin (BSA) are investigated. The binding constants (Ka) between ECG and BSA are 1.20 Ч 106 (17°C), 1.38 Ч 106 (27°C), and 5.69 x 106 L mol-1 (37°C), and the number of binding sites (n) were 1.14...
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| Format: | Article |
| Language: | English |
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University of Belgrade, University of Novi Sad
2011-01-01
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| Series: | Archives of Biological Sciences |
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| Online Access: | http://www.doiserbia.nb.rs/img/doi/0354-4664/2011/0354-46641102325Z.pdf |
| _version_ | 1819124690241716224 |
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| author | Zhao Jinyao Jiang Xinyu Liu Xin Ren Fenglian |
| author_facet | Zhao Jinyao Jiang Xinyu Liu Xin Ren Fenglian |
| author_sort | Zhao Jinyao |
| collection | DOAJ |
| description | The effects of temperature and common ions on binding (-)-epicatechin gallate (ECG) to bovine serum albumin (BSA) are investigated. The binding constants (Ka) between ECG and BSA are 1.20 Ч 106 (17°C), 1.38 Ч 106 (27°C), and 5.69 x 106 L mol-1 (37°C), and the number of binding sites (n) were 1.14, 1.15, and 1.26, respectively. These results showed that the increasing temperature improves the stability of the ECG-BSA system, which results in a higher binding constant and the number of binding sites of the ECG-BSA system. The presence of Co2+ and Zn2+ ions decreased the binding constants (Ka) and the number of binding sites (n) of ECG-BSA complex. However, the presence of Cu2+ and Ni2+ increased the affinity of ECG for BSA largely. The positive ΔH and positive ΔS indicated that hydrophobic forces might play a major role in the binding between ECG and BSA. |
| first_indexed | 2024-12-22T07:28:15Z |
| format | Article |
| id | doaj.art-570c9be028d744a4979115d451840b26 |
| institution | Directory Open Access Journal |
| issn | 0354-4664 |
| language | English |
| last_indexed | 2024-12-22T07:28:15Z |
| publishDate | 2011-01-01 |
| publisher | University of Belgrade, University of Novi Sad |
| record_format | Article |
| series | Archives of Biological Sciences |
| spelling | doaj.art-570c9be028d744a4979115d451840b262022-12-21T18:34:05ZengUniversity of Belgrade, University of Novi SadArchives of Biological Sciences0354-46642011-01-0163232533110.2298/ABS1102325ZInvestigation of the effects of temperature and ions on the interaction between ECG and BSA by the fluorescence quenching methodZhao JinyaoJiang XinyuLiu XinRen FenglianThe effects of temperature and common ions on binding (-)-epicatechin gallate (ECG) to bovine serum albumin (BSA) are investigated. The binding constants (Ka) between ECG and BSA are 1.20 Ч 106 (17°C), 1.38 Ч 106 (27°C), and 5.69 x 106 L mol-1 (37°C), and the number of binding sites (n) were 1.14, 1.15, and 1.26, respectively. These results showed that the increasing temperature improves the stability of the ECG-BSA system, which results in a higher binding constant and the number of binding sites of the ECG-BSA system. The presence of Co2+ and Zn2+ ions decreased the binding constants (Ka) and the number of binding sites (n) of ECG-BSA complex. However, the presence of Cu2+ and Ni2+ increased the affinity of ECG for BSA largely. The positive ΔH and positive ΔS indicated that hydrophobic forces might play a major role in the binding between ECG and BSA.http://www.doiserbia.nb.rs/img/doi/0354-4664/2011/0354-46641102325Z.pdfBovine serum albumininteractionECGtemperatureion |
| spellingShingle | Zhao Jinyao Jiang Xinyu Liu Xin Ren Fenglian Investigation of the effects of temperature and ions on the interaction between ECG and BSA by the fluorescence quenching method Archives of Biological Sciences Bovine serum albumin interaction ECG temperature ion |
| title | Investigation of the effects of temperature and ions on the interaction between ECG and BSA by the fluorescence quenching method |
| title_full | Investigation of the effects of temperature and ions on the interaction between ECG and BSA by the fluorescence quenching method |
| title_fullStr | Investigation of the effects of temperature and ions on the interaction between ECG and BSA by the fluorescence quenching method |
| title_full_unstemmed | Investigation of the effects of temperature and ions on the interaction between ECG and BSA by the fluorescence quenching method |
| title_short | Investigation of the effects of temperature and ions on the interaction between ECG and BSA by the fluorescence quenching method |
| title_sort | investigation of the effects of temperature and ions on the interaction between ecg and bsa by the fluorescence quenching method |
| topic | Bovine serum albumin interaction ECG temperature ion |
| url | http://www.doiserbia.nb.rs/img/doi/0354-4664/2011/0354-46641102325Z.pdf |
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