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

J Enzyme Inhib Med Chem. 2010 Dec;25(6):871-5. doi: 10.3109/14756360903489581.


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°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. In addition, IC(50) values of the drugs were determined by plotting Activity% vs [I].

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Binding, Competitive
  • Enzyme Inhibitors / adverse effects
  • Enzyme Inhibitors / pharmacology*
  • Erythrocytes / enzymology*
  • Glucosephosphate Dehydrogenase / antagonists & inhibitors*
  • Glucosephosphate Dehydrogenase / isolation & purification
  • Glucosephosphate Dehydrogenase / metabolism
  • Humans
  • Kinetics
  • Male
  • Pentose Phosphate Pathway / drug effects
  • Sulfur Compounds / adverse effects
  • Sulfur Compounds / pharmacology


  • Enzyme Inhibitors
  • Sulfur Compounds
  • Glucosephosphate Dehydrogenase