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|Title:||Purification and properties of glucose 6-phosphate dehydrogenase from turkey erythrocytes|
Kufrevioglu, O Irfan
|Abstract:||Glucose 6-phosphate dehydrogenase (G6PD) was purified from turkey erythrocytes by ammonium sulphate precipitation and followed by ADP Sepharose affinity gel chromatography. The yield was 49.71% and specific activity of the enzyme was found to be 44.16 EU/mg protein. By gel filtration the molecular mass was found to be 75 kDa. The enzyme had an optimum pH at 9.0, and optimum temperature at 50oC. Km and Vmax for NADP+ and glucose 6- phosphate (G6-P) as substrates were also determined and effects of inhibitors such as ATP, NADH and NADPH were examined.|
|Appears in Collections:||IJBB Vol.40(1) [February 2003]|
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