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Bull Environ Contam Toxicol. 2013 Nov;91(5):577-82. doi: 10.1007/s00128-013-1111-7. Epub 2013 Sep 26.

Effect of perfluorooctane sulfonate on the conformation of wheat germ acid phosphatase.

Author information

1
College of Biology and Environmental Engineering, Zhejiang Shuren University, Hangzhou, 310015, Zhejiang, China, dm25xu@163.com.

Abstract

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.

PMID:
24068464
DOI:
10.1007/s00128-013-1111-7
[Indexed for MEDLINE]
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