Purification and properties of glucose 6-phosphate dehydrogenase from turkey erythrocytes

Yilmaz H., Çiftçi M., BEYDEMİR Ş., Bakan E., KÜFREVİOĞLU Ö. İ.

Indian Journal of Biochemistry and Biophysics, cilt.40, sa.1, ss.62-65, 2003 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 40 Sayı: 1
  • Basım Tarihi: 2003
  • Dergi Adı: Indian Journal of Biochemistry and Biophysics
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.62-65
  • Anadolu Üniversitesi Adresli: Evet

Özet

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.