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Fluorescence Spectroscopy Study on the Interaction between Evodiamine and Bovine Serum Albumin
Joint Authors
Tan, Mingxiong
Gu, Yunqiong
Liang, Weijiang
Luo, Xujian
Source
Issue
Vol. 2013, Issue 2013 (31 Dec. 2013), pp.1-6, 6 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2012-12-20
Country of Publication
Egypt
No. of Pages
6
Main Subjects
Abstract EN
The interaction of evodiamine (Evo) with bovine serum albumins (BSAs) at different two temperatures (298 and 310 K) was investigated by means of fluorescence spectroscopy.
The experimental results showed that Evo binds with BSA via a static quenching procedure with association constants K of 1.61×106 L/mol at 298 K and 6.78×105 L/mol at 310 K.
The number of bound Evo molecules per protein is 1.31 at 298 K and 1.33 at 310 K.
The results suggested that Evo reacts with BSA chiefly through hydrophobic and electrostatic interactions, and it does not alter the α-helical nature of BAS.
American Psychological Association (APA)
Tan, Mingxiong& Liang, Weijiang& Luo, Xujian& Gu, Yunqiong. 2012. Fluorescence Spectroscopy Study on the Interaction between Evodiamine and Bovine Serum Albumin. Journal of Chemistry،Vol. 2013, no. 2013, pp.1-6.
https://search.emarefa.net/detail/BIM-462218
Modern Language Association (MLA)
Tan, Mingxiong…[et al.]. Fluorescence Spectroscopy Study on the Interaction between Evodiamine and Bovine Serum Albumin. Journal of Chemistry No. 2013 (2013), pp.1-6.
https://search.emarefa.net/detail/BIM-462218
American Medical Association (AMA)
Tan, Mingxiong& Liang, Weijiang& Luo, Xujian& Gu, Yunqiong. Fluorescence Spectroscopy Study on the Interaction between Evodiamine and Bovine Serum Albumin. Journal of Chemistry. 2012. Vol. 2013, no. 2013, pp.1-6.
https://search.emarefa.net/detail/BIM-462218
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-462218