| Lactate dehydrogenase (LDH) is an enzyme EC (1. 1.1.27) that functions in anaerobic glucose metabolism and glucose synthesis (1). LDH is present in a wide variety of organisms including plants and animals (2). LDH has known effectors like lactate , pyruvate, NAD+, NADH, pH, buffers composition, ionic strength(4), fructose 1,6 bisphosphate, divalent cations such as Mn2+ or Co2+ (5). Proline and trimethylamine oxid (2µ) also affect the activity of LDH(6). Drugs like antipyretic and anti-inflammatory were reported to affect lactate dehyydrogenase activity (7,8). In this study we study the effect of some antipyretic drugs ( aspegic, paracetamol, diclofenac) and anti-inflammatory drugs( hydrocortisone) on the activity of LDH and the result reveled that aspegic and paracetamol increased the activity of LDH for 2-folds,diclofenac for 1-fold and hydrocortisone for 1.8-fold, and only the actiavation in the presence of paracetamol was concentration dependant. The measurement of kinetic parameter reveled that LDH do not obeys Mechelis-Menten equation. Aspegic and paracetamol increased the km values at approximant low conc. of pyruvate and decreases the km values for approximant 10- fold at high conc. of pyruvate , while diclofenac increases the km values at all conc. of pyruvate .On the other hand hydrocortisone at as a moderate activator for LDH. This difference in the effect of these drugs on the activity of LDH could be due to the difference in the polarity of the drugs.Key word: lactate dehydrogenase, LDH, aspegic, paracetamol, diclofenac, hydrocortisone ,inhibitor ,activator . |