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Articles 1 - 12 of 12
Full-Text Articles in Physical Sciences and Mathematics
Impacts Of Some Metal Ions On Glutathione S-Transferase In The Liver Of Chalcalburnus Tarichi: An Endemic Species Of Lake Van, Muhammet Serhat Özaslan, Mehmet Çi̇ftci̇
Impacts Of Some Metal Ions On Glutathione S-Transferase In The Liver Of Chalcalburnus Tarichi: An Endemic Species Of Lake Van, Muhammet Serhat Özaslan, Mehmet Çi̇ftci̇
Turkish Journal of Chemistry
Glutathione-S-transferase (GSTs) is a multifunctional enzyme that provides homeostasis by catalyzing the first step of the formation of mercapturic acid, the end product in detoxification metabolism. They can prevent reactive electrophilic compounds from harming the body by covalently binding the same type of compounds to each other. In this study, we determined the in vitro inhibitory effects of metal ions such as Cu2+, Cd2+, Ag+, and Co2+ on GST enzyme activity. For this aim, GST was purified from C. tarichi Pallas liver with 37.36% yield and 29.304 EU/mg specific activity using the chromatographic method. The Vmax values of liver GST …
Induction Of Lutein Production In Scenedesmus Obliquusunder Different Culture Conditions Prior To Its Semipreparative Isolation, Ayşegül Erdoğan, Ayça Büşra Karataş, Zeli̇ha Demi̇rel, Meltem Dalay
Induction Of Lutein Production In Scenedesmus Obliquusunder Different Culture Conditions Prior To Its Semipreparative Isolation, Ayşegül Erdoğan, Ayça Büşra Karataş, Zeli̇ha Demi̇rel, Meltem Dalay
Turkish Journal of Chemistry
Microalgae with their improved growth rates and accumulation of high-value-added products make their commercial production attractive. Among them, lutein, which is a carotenoid, plays a very important role due to its various applications in the food and pharmaceutical industry. Induction of its biosynthesis can be triggered by various stress conditions like light. In this study, three different light intensities (50,150 and 300 μmol photons/m2s) and aeration rates (1, 3, and 5 L/min) were utilized to induce the lutein biosynthesis and biomass productivity in Scenedesmus obliquus. Lutein was isolated by preparative chromatography using a semiprep C30 column (10 × 250 mm, …
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 …
Partial Purification And Biochemical Characterization Of An Extremely Thermo- And Ph-Stable Esterase With Great Substrate Affinity, Esra Özbek, Yakup Kolcuoğlu, Leyla Konak, Ahmet Çolak, Fulya Öz
Partial Purification And Biochemical Characterization Of An Extremely Thermo- And Ph-Stable Esterase With Great Substrate Affinity, Esra Özbek, Yakup Kolcuoğlu, Leyla Konak, Ahmet Çolak, Fulya Öz
Turkish Journal of Chemistry
An esterase from a thermophilic bacterium, Geobacillus sp. DF20, was partially purified. Final purification factor was found to be 64.5-fold using Q-Sepharose ion exchange column chromatography. Native polyacrylamide gel electrophoresis indicated the presence of a single active esterase. The substrate specificity of this esterase was high for p-nitrophenyl butyrate (pNPB) substrate. The optimum pH and temperature for the enzyme activity were 7.0 and 50 ^°C, respectively. The pH and heat stability profiles show that this enzyme is more stable under neutral conditions at 50 ^°C. K_m and V_{max} values for this esterase acting on pNPB were 0.12 mM and 54.6 …
Purification And Partial Characterization Of Catalase From Chicken Erythrocytes And The Effect Of Various Inhibitors On Enzyme Activity, Tüli̇n Aydemi̇r, Kevser Kuru
Purification And Partial Characterization Of Catalase From Chicken Erythrocytes And The Effect Of Various Inhibitors On Enzyme Activity, Tüli̇n Aydemi̇r, Kevser Kuru
Turkish Journal of Chemistry
Catalase plays a major role in the protection of tissues from the toxic effects of H_{2}O_{2} and partially reduced oxygen species. A nearly 136-fold enzyme purification was obtained from chicken erythrocyte by acetone precipitation, ethanol-chloroform treatment, CM-cellulose and Sephadex G-200 chromatography. The specific activity of purified enzyme was 42,556 U/mg. The molecular weight of the native chicken erythrocyte catalase was estimated at 240 kDa by gel filtration. SDS-gel electrophoresis results indicated that chicken erythrocyte catalase consists of four apparently identical subunits, with a molecular weight of around 57.5 kDa. The optical spectrum of the purified enzyme shows a Soret band …
Purification And Characterization Of Glucose 6-Phosphate Dehydrogenase From Sheep Liver, Vedat Türkoğlu, Si̇nan Aldemi̇r, Mehmet Çi̇ftçi̇
Purification And Characterization Of Glucose 6-Phosphate Dehydrogenase From Sheep Liver, Vedat Türkoğlu, Si̇nan Aldemi̇r, Mehmet Çi̇ftçi̇
Turkish Journal of Chemistry
Glucose 6-phosphate dehydrogenase (D-glucose 6-phosphate: NADP^{+} oxidoreductase, EC 1.1.1.49; G6PD) was purified from sheep liver by a simple and rapid method. The purification process consisted of two steps: preparation of the homogenate, and 2', 5'-adenosine diphosphate (ADP) Sepharose 4B affinity chromatography. Through the use of these two consecutive steps, the enzyme was purified with a yield of 35.6% and 1,920 fold, having the specific activity of 11.2 enzyme units (EU/mg protein). A K_{M} of 0.176 mM and a V_{\max} of 0.0179 EU/ml were obtained for G6-P, and 0.0194 mM and 0.0223 EU/ml for NADP^{+}. Enzymatic activity was measured spectrophotometrically according …
Isolation And Characterization Of A Smectite As A Micro-Mesoporous Material From A Bentonite, Müşerref Önal, Yüksel Sarikaya, Tülay Alemdaroğlu, İhsan Bozdoğan
Isolation And Characterization Of A Smectite As A Micro-Mesoporous Material From A Bentonite, Müşerref Önal, Yüksel Sarikaya, Tülay Alemdaroğlu, İhsan Bozdoğan
Turkish Journal of Chemistry
A procedure was assessed for obtaining an optimum amount of a micro-mesoporous material known as smectite from Reşadiye (Tokat/Turkey) bentonite. The procedure, which will permit a better economic evaluation of the Reşadiye reserves, is based on successive settlements of bentonite suspensions during various time intervals. To characterize the original bentonite, its fractions and the high purity smectite product, X-ray diffraction, differential thermal analysis, thermogravimetric analysis, scanning electron microscopy and nitrogen adsorption-desorption techniques were used. The original bentonite contained 50% by mass sodium-rich smectite (NaS) and 10% by mass NaCa-smectite (NaCaS). It also contained illite, clinoptilolite, analcime, feldspar, calcite, dolomite, quartz …
Partially Purification And Characterization Of Polyphenol Oxidase Of Quince, Hülya Yağar, Ayten Sağiroğlu
Partially Purification And Characterization Of Polyphenol Oxidase Of Quince, Hülya Yağar, Ayten Sağiroğlu
Turkish Journal of Chemistry
Polyphenol oxidase (PPO, EC 1.14.18.1) was extracted from quince (Cydonia oblonga) by using 0.1 M phosphate buffer, pH 6.8. The polyphenol oxidase of quince was partially purified by (NH_{4})_{2}SO_{4} and dialysis. Substrate specificity experiments were carried out with catechol, pyrogallol, L-DOPA, p-cresole and tyrosine. Catechol was the most suitable substrate compound for quince PPO. The Michaelis constants were 4.54 mM, 7.35mM and 17.8 mM for catechol, pyrogallol and L-DOPA, respectively at 25^oC. The optimum pH and temperature were determined with the specific substrate catechol as 8.0 and 40$^oC, respectively. Of eight inhibitors tested L-cysteine, ascorbic acid and potassium cyanide were …
Non-Covalent Immobilization Of Quince (Cydonia Oblonga) Polyphenol Oxidase, Hülya Yağar, Ayten Sağiroğlu
Non-Covalent Immobilization Of Quince (Cydonia Oblonga) Polyphenol Oxidase, Hülya Yağar, Ayten Sağiroğlu
Turkish Journal of Chemistry
A partially purified polyphenol oxidase from quince (Cydonia oblonga) was immobilized on bentonite by simple adsorption at pH 6.8. The properties of the immobilized enzyme were compared to those of the free enzyme. Optimum pH and temperature were determined to be 9.0 and 45°C, respectively, showing the alteration of pH and temperature profiles by immobilization. No drastic change was observed in the K_m value after immobilization. Catechol, L-DOPA, p-cresole and pyrogallol were tested as substrates. Thermal and storage stability and reusability experiments were carried out. It was observed that the immobilized enzyme had storage stability for a period of one …
A Comparative Study On The Recovery Of Ecori Endonuclease From Two Different Genetically Modified Strains Of Escherichia Coli, Candan Tamerler, Zeynep İlsen Önsan, Betül Kirdar
A Comparative Study On The Recovery Of Ecori Endonuclease From Two Different Genetically Modified Strains Of Escherichia Coli, Candan Tamerler, Zeynep İlsen Önsan, Betül Kirdar
Turkish Journal of Chemistry
A laboratory scale procedure developed for the purification of EcoRI restriction endonuclease was applied to two different Escherichia coli} strains, E. coli 294 and E. coli M5248, which are genetically modified to overproduce the enzyme. The purification method consisted of three successive chromatographic steps including phosphocellulose and hydroxyapatite columns and further fractionation in a second phosphocellulose column. It was shown that the second phosphocellulose separation can be omitted in the case of E. coli 294. Quality control tests indicated enzyme preparations free of contaminants and endo- or exo-nucleases. The yields obtained at the final stage of the purification were 1.3x10^{5} …
Purification And Partial Characterisation Of Superoxide Dismutase From Chicken Erythrocytes, Tüli̇n Aydemi̇r, Leman Tarhan
Purification And Partial Characterisation Of Superoxide Dismutase From Chicken Erythrocytes, Tüli̇n Aydemi̇r, Leman Tarhan
Turkish Journal of Chemistry
Superoxide dismutase (SOD), which plays a very important role in protecting organisms from oxygen toxicity, was purified from chicken erythrocyte and partially characterised. Erythrocyte membranes were disintegrated via freeze-thaw methods in the presence of Triton X-100. Following ethanol precipitation, SOD-containing solution was applied to DEAE-cellulose and then Sephadex G-100 gel columns. Chicken erythrocyte SOD was purified 508-fold with a specific activity of 8,480 units per mg. The molecular weight was estimated to be 30.6 kDa \pm 0.4 by gel filtration. The enzyme was composed of two subunits of equal size and contained one atom of copper and one atom of …