Abstract
A selective and sensitive method to study the interaction between hydroxylated polybrominated diphenyl ethers (OH-PBDEs) and protein disulfide isomerase (PDI) was established in this assay. In this report, 3,3′,5-triiodo-thyronine (T3) was conjugated with fluorescein (FITC) as a fluorescence probe (F-T3) to study the competitive binding interaction of OH-PBDEs to PDI, which was observed to exhibit T3 binding activity. The findings suggest that some OH-PBDEs have the potential of binding to PDI, and they share the same binding site as T3 to PDI; moreover, OH-PBDEs were able to act as a competitive inhibitor in PDI binding to T3.
Original language | English |
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Pages (from-to) | 8106-8109 |
Number of pages | 4 |
Journal | Analytical Methods |
Volume | 6 |
Issue number | 20 |
DOIs | |
Publication status | Published - 21 Oct 2014 |
Scopus Subject Areas
- Analytical Chemistry
- General Chemical Engineering
- General Engineering