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Full-Text Articles in Physical Sciences and Mathematics
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 …