Purification, characterization and kinetic properties of glucose 6-phosphate dehydrogenase from Polygonum cognatum Meissn leaves

Demir H., BEYDEMİR Ş., Çiftçi M.

Asian Journal of Chemistry, vol.21, no.1, pp.517-527, 2009 (SCI-Expanded) identifier

  • 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.