Angiotensin-CONVERTING ENZYME ((ACE)) (EC: 3.4.15.1) is a peptidyl dipeptide hydrolase that removes the carboxyl terminal (His-Leu) from angiotensin I to produce the octapeptide angiotensin n. Due to the importance of (ACE) and its active site-directed inhibitors in the pathogenesis and treatment of cardiovascular disorders such as hypertension and heart failure, (ACE) purification and assay are of clinical and commercial as well as scientific interest. In the present study it was attempted to purify (ACE) faster and simpler. Purification procedure was finally performed in three steps. After homogenization and centrifugation, (ACE) was solubilized from pellet using Nonidet-P40, a non-ionic detergent. The supernatant solution brought to 50% and 70% saturation concentration of ammonium sulfate. After ammonium sulfate precipitation, the supernatant solution was used to purify (ACE) by Q-Sepharose HP as a strong anion exchanger and then by Sephacryl HR S200 (gel filtration). After these steps, (ACE) purification was confirmed by PAGEand SOS-PAGE. The molecular weight found for (ACE) was 175 KO. Final specific activity was 39.1 units/mg which was achieved through 651 fold purification and the activity' recovered was 5.2%. After purification, Km of (ACE) for Hippuryl-Histidyl-Leucine, a synthetic substrate, was 2.17 mM. Concentrations between 0.001- 0.1 mM of Captopril, a competitive inhibitor, inhibited (ACE) almost completely. Optimal pH determined for (ACE) activity was 8.3. Incubation temperature above 37oc decreased (ACE) activity remarkably. (ACE) purification in three steps (previously often in 5 steps), a decrease in purification steps, procedure time and expenditure and also acceptable activity and yield, were all due to using resins with high resolution and also FPLC (Fast Protein Liquid Chromatography) system which, finally, facilitated the chromatographic procedures.