Purification and characterization of 6-PGD from quail liver - Hamzah, Salih; Çiftçi, Mehmet
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In this study, 6-phosphogluconate dehydrogenase (6PGD) enzyme was purified from the quail liver by using ammonium sulphate precipitation, and 2', 5'-ADP Sepharose 4B affinity chromatography methods, with specific activities 14.6 EU/mg, 89% yield and 112 purification fold. Enzyme activity was measured spectrophotometrically at 340 nm. SDS-PAGE checked the purity of the enzyme. The molecular weight of purified enzyme by the SDS-PAGE method was calculated to be 44 KDa. Protein determination was performed by the Bradford method. For the enzyme optimal pH (8.0), stable pH (8.0), optimum ionic…mehr

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Produktbeschreibung
In this study, 6-phosphogluconate dehydrogenase (6PGD) enzyme was purified from the quail liver by using ammonium sulphate precipitation, and 2', 5'-ADP Sepharose 4B affinity chromatography methods, with specific activities 14.6 EU/mg, 89% yield and 112 purification fold. Enzyme activity was measured spectrophotometrically at 340 nm. SDS-PAGE checked the purity of the enzyme. The molecular weight of purified enzyme by the SDS-PAGE method was calculated to be 44 KDa. Protein determination was performed by the Bradford method. For the enzyme optimal pH (8.0), stable pH (8.0), optimum ionic strength (600 mM in Tris-HCl) optimal temperature (60°C) were determined. In addition KM and Vmax values for 6-phosphogluconate (6-PGA) and NADP+ were calculated as 0.058 and 0.0015 mM; 0.0078 and 0.057 EU/ml respectively.
Autorenporträt
I was born in Erbil 1978. I completed my primary, secondary, high school in Erbil. I entered the college of the science department of chemistry Salahhadin University, graduated in 2001. In 2003, I used to work in the laboratory of the hospital doing chemical testing. In February 2015 started post-graduation from Bingol University, Biochemistry.