期刊
BULLETIN OF ENVIRONMENTAL CONTAMINATION AND TOXICOLOGY
卷 91, 期 5, 页码 577-582出版社
SPRINGER
DOI: 10.1007/s00128-013-1111-7
关键词
PFOS; Acid phosphatase; Fluorescence spectroscopy; Conformation
资金
- National Natural Science Foundation of China [20907046]
- Undergraduate Scientific and Technological Innovation Project of Zhejiang Province [2010R420014, 2012R420012]
Fluorescence spectroscopy was used to study the quenching mechanism, the type of force and the binding sites of perfluorooctane sulfonate (PFOS) on wheat germ acid phosphatase (ACPase). The results showed that the quenching effect of PFOS on ACPase was mainly due to a static quenching mechanism that occurred via the formation of hydrogen bonds and van der Waals forces. The results from synchronous fluorescence spectroscopy demonstrated that PFOS interacts with ACPase close to the tryptophan residues. In addition, synchronous fluorescence spectroscopy also showed that PFOS increases the hydrophobicity of the microenvironment of the tyrosine residues, hence decreasing the local polarity.
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