In this study, a lipase from the liver of Cyprinus carpi Linnaeus (1758) living in Todurge Lake (Sivas) was purified with purification parameters of 90.38 mu mol/dk.mg protein specific activity and 75.50 fold purity. The purification procedure consisted of preparation of homogenate, precipitation with polyethylene glycol-6000 (PEG-6000) and chromatographic techniques including in Q sepharose, sephacryl S 200 HR and phenyl sepharose CL-4B, respectively. The purified lipase showed a single band with approximately a molecular weight of 74 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). pH and temperature optimums for the purified enzyme were determined as 8 and 37 degrees C using p-nitrophenyl butirate (p-NPB) as substrate. K-m and V-max values were found as 0.17 mM p-NPB and 2.6 mu mol/ml.dk, respectively. It was observed that surface active agents, such as sodium dodecyl sulfate (SDS), Triton X-100 and Nataurocholate act as inhibitor on lipase activity.