Spectroscopic investigation on the interaction of Cr(VI) with bovine serum albumin |
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Authors: | Zhang Pengjun Lan Ping Ma Yuening Gao Yan Chen Hao Fang Qian Zong Wansong Liu Rutao |
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Institution: | Shandong Key Laboratory of Water Pollution Control and Resource Reuse, School of Environmental Science and Engineering, Shandong University, China-America CRC for Environment & Health, Shandong Province, Jinan 250100, People's Republic of China. |
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Abstract: | The interaction of potassium dichromate (Cr(VI)) with bovine serum albumin (BSA) was investigated by fluorescence, synchronous fluorescence, resonance light scattering (RLS), ultraviolet-visible absorption, and circular dichroism (CD) spectroscopies under simulated physiological conditions. The experimental results showed that Cr(VI) could quench the intrinsic fluorescence of BSA following a static quenching process, which indicates the formation of a Cr(VI)-BSA complex. The binding constant (KA) and binding site (n) were measured at different temperatures. The spectroscopic results also revealed that the binding of Cr(VI) to BSA can lead to the loosening of the protein conformation and can change the microenvironment and skeleton of BSA. |
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Keywords: | Bovine Serum Albumin Cr(VI) Interaction Spectroscopic Techniques |
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