PURIFICATION OF BOVINE MILK LIPOPROTEIN-LIPASE WITH AID OF DETERGENT
- 1 January 1977
- journal article
- research article
- Vol. 55 (3) , 187-191
Abstract
A simple method is described for the purification of bovine milk lipoprotein lipase, EC 3.1.1.3 based on affinity chromatography on agarose containing covalently linked heparin and the use of non-ionic detergent, Triton X-100. By this procedure mg amounts of detergent-free lipoprotein lipase with a specific activity of 28.9 mmoles free fatty acid/mg protein/h can be obtained. The apparent MW of the polypeptide as determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate is 55,000. The purified triacylglycerol lipase also hydrolyzes monoacylglycerol, but the activity against this lipid is 40 times lower than that against triacylglycerol.This publication has 7 references indexed in Scilit:
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