Purification and Properties of Bovine Aortic Lipoprotein Lipase

Abstract

Lipoprotein lipase of bovine aortic intima has been purified to homogeneity by affinity chromatography on heparin-Sepharose. As determined by polyacrylamide gel electrophoresis in sodium dodecyl sulfate, the purified enzyme had a molecular weight of approximately 60,000, required apolipoprotein C-II for activity and was inhibited by 1.0 M NaCI. Optimum lipolytic activity was in the pH range of 8.0-8.5. Bovine skimmed milk lipoprotein lipase was also purified and its properties compared to those of the aortic enzyme. Based on these comparative studies, we conclude that bovine aortic and milk lipoprotein lipase have similar physio-chemical properties.