Antioxidant activity of bovine serum albumin binding amino acid Schiff-bases metal complexes

2007 ◽  
Vol 18 (11) ◽  
pp. 1416-1418 ◽  
Author(s):  
Rong Min Wang ◽  
Juan Juan Mao ◽  
Jing Feng Song ◽  
Cai Xia Huo ◽  
Yu Feng He
2015 ◽  
Vol 7 (12) ◽  
pp. 5096-5102 ◽  
Author(s):  
Ali Saber Abdelhameed ◽  
Amer M. Alanazi ◽  
Adnan A. Kadi

Finasteride and bovine serum albumin binding is investigated and used for simple, accurate quantification of finasteride in tablets.


2016 ◽  
Vol 157 ◽  
pp. 80-93 ◽  
Author(s):  
Luciana G. Naso ◽  
Luis Lezama ◽  
María Valcarcel ◽  
Clarisa Salado ◽  
Patricia Villacé ◽  
...  

2007 ◽  
Vol 11 (07) ◽  
pp. 475-480 ◽  
Author(s):  
Nelli H. Karapetyan ◽  
Lusine R. Aloyan ◽  
Robert K. Ghazaryan ◽  
Yevgeni Mamasakhlisov

Bovine serum albumin complexes with water-soluble cationic porphyrins, Cu - and Co-meso-tetra(4- N -hydroxyethylpyridyl)porphyrins ( CuT4OEPyP , CoT4OEPyP ), and their 3- N -analogs, meso-tetra(3- N -hydroxyethylpyridyl)porphyrins ( CuT3OEPyP , CoT3OEPyP ), have been investigated. The porphyrin-bovine serum albumin binding was monitored by the absorption in the visible region at 400-460 nm. The stoichiometry of binding and the binding constants of the porphyrins to bovine serum albumin were determined using binding isotherms and Scatchard plots. The K b values obtained for these porphyrin- bovine serum albumin complexes are 1.7 × 105 M −1, 3.2 × 105 M −1, 1.4 × 105 M −1 and 3 × 105 M −1 respectively. Binding constants are sensitive to pH and ionic strength of the solution.


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