Purification, Characterization and Kinetic Properties of Glucose 6-Phosphate Dehydrogenase from Polygonum cognatum Meissn Leaves

Demir H., Beydemir S., Ciftci M.

ASIAN JOURNAL OF CHEMISTRY, cilt.21, ss.517-527, 2009 (SCI İndekslerine Giren Dergi) identifier identifier

  • Cilt numarası: 21 Konu: 1
  • Basım Tarihi: 2009
  • Sayfa Sayıları: ss.517-527


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 degrees C. Stable pH, optimum pH, optimum temperature, subunit molecular weight, native form molecular weight, K-m and v(max) 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.