The interaction between cationic porphyrin, a potential valuable antitumor and antibiotic drug, and human serum albumin (HSA) was investigated using spectroscopy methods. The binding constants were obtained using fluorescence quenching method (K SV ΒΌ (3.24 AE 0.29) Γ 10 4 M Γ1 ) and surface plasmon
Study of caffeine binding to human serum albumin using optical spectroscopic methods
β Scribed by Qiong Wu; ChaoHong Li; YanJun Hu; Yi Liu
- Book ID
- 107348875
- Publisher
- SP Science China Press
- Year
- 2009
- Tongue
- English
- Weight
- 691 KB
- Volume
- 52
- Category
- Article
- ISSN
- 1674-7291
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The interaction between Puerarin with human serum albumin has been studied for the first time by spectroscopic methods including fluorescence quenching technology, circular dichroism (CD) spectroscopy and Fourier transform infrared (FT-IR) spectroscopy under simulative physiological conditions. The
## Abstract Flavonols are plant pigments that are ubiquitous in nature. Quercetin (3,3β²,4β²,5,7βpentahydroxyflavone) and other related plant flavonols have come into recent prominence because of their usefulness as anticancer, antitumor, antiβAIDS, and other important therapeutic activities of signi