Preparation of a Homogenous and Stable form of Bovine Milk Lipoprotein Lipase

Abstract

Lipoprotein lipase was purified to homogeneity from bovine skim milk by a two-step procedure using chromatography on heparin-Sepharose. As determined by gradient-polyacrylamide gel electrophoresis in sodium dodecyl sulfate, purified lipoprotein lipase showed a single band with an apparent molecular weight of 55,000. The use of Triton N-101 in the washing buffers was the major improvement from previously reported purification procedures that resulted in a stable homogeneous preparation of the enzyme.