Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
870069 | Biosensors and Bioelectronics | 2006 | 5 Pages |
Using a fluorescein di-β-d-galactopyranoside (FDG) substrate we show that in live cells of an estrogen-sensitive yeast strain RMY/ER-ERE with human estrogen receptor (ERα) gene and the lacZ gene which encodes β-galactosidase, the uptake of 17β-estradiol (E2) and the subsequent production of β-galactosidase enzyme occur quite rapidly, with maximal enzyme-catalyzed product formation evident after about 30 min of exposure to E2. This finding which agrees with the well-known rates of enzyme-catalyzed reactions could have implications for shortening the duration of environmental sample screening and monitoring regimes using yeast-based estrogen assays, and the development of biosensors for environmental estrogens to complement quantification methods.