Purification and properties of glucose 6-phosphate dehydrogenase from coriander (Coriandrum sativum) leaves

DEMIR H., BEYDEMIR O., CIFTCI M., Kufrevioglu O.

JOURNAL OF FOOD BIOCHEMISTRY, cilt.28, sa.2, ss.155-168, 2004 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 28 Sayı: 2
  • Basım Tarihi: 2004
  • Doi Numarası: 10.1111/j.1745-4514.2004.tb00062.x
  • Dergi Adı: JOURNAL OF FOOD BIOCHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.155-168
  • Atatürk Üniversitesi Adresli: Evet

Özet

Glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate: NADP(+) oxidoreductase, EC 1.1.1.49; G6PD) was purified from coriander (Coriandrum sativum) leaves; the kinetic behavior and some properties of the enzyme were also investigated. The purification was done at 4C and involved two steps: ammonium sulfate fractionation, and DEAF-Sephadex A50 ion exchange chromatography. The enzyme was obtained with a yield of 26.4% and had a specific activity of 1.826 U/mg protein. Optimum pH, stable pH, optimum temperature, molecular weight, K-M and V-max values for NADP(+) and glucose 6-phosphate (G6-P) were also determined.