Purification of bovine milk lipoprotein lipase with the aid of detergent.
The present study describes a simple method for the purification of bovine milk lipoprotein lipase based on affinity chromatography on agarose containing covalently linked heparin and the use of a non-ionic detergent, Triton X-100. By this procedure miligram amounts of detergent-free lipoprotein-ionic lipase with a specific activity of 28.9 mmoles free fatty acid/mg protein/mg protein/hour can be obtained. The apparent molecular weight of the polypeptide as determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate is 55,000. The purified triacylglycerol lipase also hydrolyzes monoacylglycerol, but the activity against this lipid is 40 times lower than that against triacylglycerol.
D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D003902:Detergents; D008071:Lipoprotein Lipase / Q000302:isolation & purification*; D008722:Methods; D008892:Milk / Q000201:enzymology*; D011092:Polyethylene Glycols; D011485:Protein Binding
D003902:Detergents; D011092:Polyethylene Glycols; D008071:Lipoprotein Lipase