Purification and characterization of glucose 6-phosphate dehydrogenase from sheep erythrocytes and inhibitory effects of some antibiotics on enzyme activity

Beydemir S., Ciftci M., Kufrevioglu O.

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.17, sa.4, ss.271-277, 2002 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 17 Sayı: 4
  • Basım Tarihi: 2002
  • Doi Numarası: 10.1080/1475636021000010941
  • Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.271-277
  • Anahtar Kelimeler: glucose 6-phosphate dehydrogenase, drug, sheep, erythrocyte, GLUCOSE-6-PHOSPHATE-DEHYDROGENASE
  • Atatürk Üniversitesi Adresli: Evet

Özet

Glucose 6-phosphate dehydrogenase (D-glucose 6-phosphate: NADP(+) oxidoreductase, EC 1.1.1.49; G6PD) was purified from sheep erythrocytes, using a simple and rapid method. The purification consisted of three steps; preparation of haemolysate, ammonium sulphate fractionation and 2', 5'-ADP Sepharose 4B affinity chromatography. The enzyme was obtained with a yield of 37.1% and had a specific activity of 4.64 U/mg proteins. Optimal pH, stable pH, molecular weight, and K-M and V-max values for NADP(+) and glucose 6-phosphate (G6-P) substrates were also determined for the enzyme.