Purification and characterization of mitochondrial thioredoxin reductase enzyme from rainbow trout (Oncorhynchus mykiss) liver and investigation of the in vitro effects of some metal ions on the enzyme
Özet
Thioredoxin reductase (E.C 1.6.4.5.; TrxR) is an enzyme belonging to the flavoprotein family of pyridine
nucleotide-disulfide oxidoreductases. In this study, mitochondrial TrxR enzyme was purified from rainbow trout mitochondria.
Thanks to the 2 consecutive procedures (preparation of homogenate and 2’,5’-ADP Sepharose 4B affinity
chromatography), the enzyme, having the specific activity of 11.9 EU mg protein-1, was purified with a yield of 2.38%
and 672-fold. The purity of the enzyme was monitored and the molecular weight of its subunits was calculated as 70
kDa by SDS-PAGE. The native molecular mass of the enzyme was found to be approximately 151 kDa by gel filtration
chromatography. Characteristic and kinetic properties of the enzyme were also determined. Furthermore, Se 4+ , Cu 2+ ,
Co 2+ , Ni 2+ , Fe 3+ , and Al 3+ metal ions’ in vitro effects on mitochondrial TrxR purified from rainbow trout was investigated.
While Se 4+ ion increased the enzyme activity, all of the other metal ions used in this study showed an inhibitory
effect.
Koleksiyonlar
- Kimya [22]
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