PURIFICATION OF LIPOPROTEIN LIPASE FROM RAT POST-HEPARIN PLASMA

1. 1. Lipoprotein lipase, which catalyses the hydrolysis of the triglyceride moiety of plasma low-density lipoproteins, has been highly purified from rat post-heparin plasma. 2. 2. The product gave a single band after acrylamide gel electrophoresis, and specific activity was not further increased by acetone fractionation or by chromatography on Sephadex G-150. 3. 3. The sedimentation coefficient was 4.85 S, and the apparent molecular weight was 72 600. 4. 4. The temperature and pH optima and the stability of the purified enzyme have been determined. The stability of the plasma enzyme is the same as that previously reported for the enzyme in adipose tissue. © 1969.