A. A. Uwakwe
Department of Biochemistry, University of Port Harcourt, Nigeria.
P.M.B. 5323, Port Harcourt, Nigeria.
M. O. Monanu
Department of Biochemistry, University of Port Harcourt, Nigeria.
P.M.B. 5323, Port Harcourt, Nigeria.
Abstract
The activity of glutathione-S-transferase of human erythrocytes was monitored spectrophotometically in the presence and absence of two analgesics (aspirin and paracetamol). Five different concentrations (1.0, 3.0, 5.0, 7.0, 9.0 and 10.0 mg/ml) of each analgesic were used which covers the reported therapeutic and toxic concentration range of the drugs. The drugs were observed to significantly (P < 0.05) inhibit the enzyme. Inhibitions greater than 42.0% were observed at 10mg/ml concentrations of the two drugs. Enzyme inhibition studies demonstrated a competitive inhibition pattern for both aspirin and paracetamol. The inhibition pattern was interpreted as indicative of a higher degree of inhibition at reduced levels of the enzyme's substrate, glutathione (GSH).
(Global Journal of Medical Science, 2004, 3 (1&2): 33-36)