IN VITRO EFFECTS OF SOME HEAVY METAL IONS ON CYTOSOLIC THIOREDOXIN REDUCTASE PURIFIED FROM RAINBOW TROUT GILL TISSUES
Yazarlar (2)
Aǧrı İbrahim Çeçen Üniversitesi, Türkiye
Prof. Dr. Müslüm KUZU
Ağrı İbrahim Çeçen Üniversitesi, Türkiye
| Makale Türü | Özgün Makale |
| Makale Alt Türü | SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale |
| Dergi Adı | Fresenius Environmental Bulletin |
| Dergi ISSN | 1018-4619 Wos Dergi Scopus Dergi |
| Dergi Tarandığı Indeksler | SCI-Expanded |
| Makale Dili | İngilizce |
| Basım Tarihi | 01-2017 |
| Cilt No | 26 |
| Sayı | 7 |
| Sayfalar | 4677 / 4683 |
| Özet |
| Thioredoxin system is formed of thioredoxin reductase (EC 1.6. 4.5.; TrxR), thioredoxin (Trx) and nicotinamide adenine dinucleotide phosphate (NADPH), and participates in cell growth, apoptosis, antioxidant defense, redox signaling, etc. In this study, cytoplasmic TrxR enzyme was purified by using heat denaturation and 2', 5'-ADP Sepharose 4B affinity chromatograph techniques from rainbow trout gill tissues. The purity and the monomer molecular weight of the enzyme were determined with SDS-PAGE. KM values for NADPH and 5, 5'-Dithiobis (2-nitrobenzoic acid), the substrates of the enzyme were calculated by means of Lineweaver-Burk graphic. Optimal pH and optimal ionic strength values were determined as 7.75 and 300 mM, respectively. Then, in vitro effects of the Ni2+, Cu2+, Pb2+, Cd2+, Sr2+, Zn2+, Mg2+, Cr3+, Fe3+, Al3+ and Ag+ metal ions on the enzyme activity were analyzed. IC50 values were determined for the ones showing inhibition effect and their Ki values were calculated by means of Cheng-Prusoff equation. |
| Anahtar Kelimeler |
| Thioredoxin Reductase | Purification | Heavy Metal | Inhibition |
