Open Access. Powered by Scholars. Published by Universities.®
Physical Sciences and Mathematics Commons™
Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 2 of 2
Full-Text Articles in Physical Sciences and Mathematics
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, İlknur Özgençli̇, Mehmet Çi̇ftci̇
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, İlknur Özgençli̇, Mehmet Çi̇ftci̇
Turkish Journal of Chemistry
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 …
Production, Purification, And Characterization Of A Thermo-Alkali Stable And Metal-Tolerant Carboxymethylcellulase From Newly Isolated Bacillus Methylotrophicus Y37, Yonca Duman, Yonca Yüzügüllü Karakuş, Arzu Sertel, Fi̇kri̇ye Polat
Production, Purification, And Characterization Of A Thermo-Alkali Stable And Metal-Tolerant Carboxymethylcellulase From Newly Isolated Bacillus Methylotrophicus Y37, Yonca Duman, Yonca Yüzügüllü Karakuş, Arzu Sertel, Fi̇kri̇ye Polat
Turkish Journal of Chemistry
A carboxymethylcellulose (CMC)-degrading bacterium was isolated from soil, identified as Bacillus methylotrophicus according to the physiological properties and analyses of 16S rRNA and a partial sequence of the gyrase A (gyrA) gene, and named as B. methylotrophicus Y37. The CMCase enzyme was purified to homogeneity by 20.4-fold with 21.73% recovery using single-step hydrophobic interaction chromatography and biochemically characterized. CMCase showed a molecular weight of approximately 50 kDa as determined by SDS-PAGE. The activity profile of the CMCase enzyme exhibited optimum activity at 45 $^{\circ}$C and pH 5.0. The activity was highly stable at alkaline pH levels. More than 90% of …