Purification and properties of glucose 6-phosphate dehydrogenase from turkey erythrocytes
Yilmaz, H.; Ciftçi, M.; Beydemir, S.ük.ü; Bakan, E.; Küfrevioğlu, O.I.
Indian Journal of Biochemistry and Biophysics 40(1): 62-65
2003
ISSN/ISBN: 0301-1208 PMID: 22900294 Document Number: 557454
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 50 degrees C. 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.