Purification of human plasma lipoprotein lipase

Abstract Human plasma lipoprotein lipase was purified in a highly active form. Addition of the non-ionic detergent Triton X-100 led to stabilization of enzyme activity during the purification procedure. Antithrombin III, the major contaminant after affinity chromatography with heparin-Sepharose 4B, could be removed by gelfiltration on Bio-Gel A-5m. The application of Tris-glycine buffer in the absence of denaturating agents allowed identification of the protein band corresponding to lipoprotein lipase activity on polyacrylamide gels.