Effects of some drugs on human erythrocyte glucose 6-phosphate dehydrogenase: an in vitro study

Akkemik E., BUDAK H., ÇİFTÇİ M.

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.25, sa.6, ss.871-875, 2010 (SCI-Expanded) identifier identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 25 Sayı: 6
  • Basım Tarihi: 2010
  • Doi Numarası: 10.3109/14756360903489581
  • Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.871-875
  • Anahtar Kelimeler: Glucose-6-phosphate dehydrogenase, erythrocyte, drugs, CELL GLUCOSE-6-PHOSPHATE-DEHYDROGENASE, 6-PHOSPHOGLUCONATE DEHYDROGENASE, ANTIBIOTICS, PURIFICATION, ENZYME, INHIBITION
  • Atatürk Üniversitesi Adresli: Evet

Özet

Inhibitory effects of some drugs on glucose 6-phosphate dehydrogenase from the erythrocytes of human have been investigated. For this purpose, at the beginning, erythrocyte glucose 6-phosphate dehydrogenase was purified 2256 times in a yield of 44.22% by using ammonium sulphate precipitation and 2',5'-ADP Sepharose 4B affinity gel. Temperature of +4 degrees C was maintained during the purification process. Enzyme activity was determined with the Beutler method by using a spectrophotometer at 340 nm. This method was utilized for all kinetic studies. Ketotifen, dacarbazine, thiocolchicoside, meloxicam, methotrexate, furosemide, olanzapine, methylprednizolone acetate, paricalcitol, ritodrine hydrochloride, and gadobenate-dimeglumine were used as drugs. All the drugs indicated the inhibitory effects on the enzyme. Ki constants for glucose 6-phosphate dehydrogenase were found by means of Lineweaver-Burk graphs. While methylprednizolone acetate showed competitive inhibition, the others displayed non-competitive inhibition.