Purification, characterization and kinetic properties of glucose 6-phosphate dehydrogenase from Polygonum cognatum Meissn leaves
Asian Journal of Chemistry, vol.21, no.1, pp.517-527, 2009 (SCI-Expanded, Scopus)
- Publication Type: Article / Article
- Volume: 21 Issue: 1
- Publication Date: 2009
- Journal Name: Asian Journal of Chemistry
- Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Page Numbers: pp.517-527
- Keywords: Characterization, Glucose 6-phosphate dehydrogenase, Polygonum cognatum Meissn
- Anadolu University Affiliated: Yes
Abstract
In the present studies, the isolation, purification and kinetic properties of glucose-6-phosphate dehydrogenase (G6PD) in the Polygonum cognatum Meissn leaves were investigated. The purification procedure was composed of three steps viz., homogenate preparation, ammonium sulfate precipitation and DEAE-Sephadex A50 ion exchange chromatography. The enzyme, having the specific activity of 1.896 EU/mg proteins, was purified with a yield of 57.6 % and 124.08 fold at 4°C. Stable pH, optimum pH, optimum temperature, subunit molecular weight, native form molecular weight, Km and vmax values for NADP and glucose 6-phosphate (G6-P) substrates were also determined for the enzyme. Enzymatic activity was spectrophotometrically measured according to Beutler's method at 340 nm.