title: 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 gel filtration 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.
mesh_terms: D002021:Buffers; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008071:Lipoprotein Lipase / Q000097:blood / Q000302:isolation & purification*; D011092:Polyethylene Glycols
chemical_list: D002021:Buffers; D011092:Polyethylene Glycols; D008071:Lipoprotein Lipase