Purification and properties of glucose 6-phosphate dehydrogenase from turkey erythrocytes
Indian Journal of Biochemistry and Biophysics, vol.40, no.1, pp.62-65, 2003 (SCI-Expanded, Scopus)
- Publication Type: Article / Article
- Volume: 40 Issue: 1
- Publication Date: 2003
- Journal Name: Indian Journal of Biochemistry and Biophysics
- Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Page Numbers: pp.62-65
- Anadolu University Affiliated: Yes
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 50°C. K m and V max 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.