The Purification of a Lipoprotein Lipase from Human Adipose Tissue
The purification of lipoprotein lipase from human adipose tissue was accomplished after successive chromatography on heparinSepharose and concanavalin A-agarose of an acetone-ether treated crude homogenate. The preparation obtained was purified 2,000-fold. A single protein with an apparent molecular weight of 60,000 daltons was obtained after solubilization of the protein with sodium dodecylsulfate in the presence of leupeptin before separation of the proteins by slab gel polyacrylamide electrophoresis. Omission of the protease inhibitor, leupeptin, resulted in breakdown of lipoprotein lipase into two small proteins of different size of 31,000 and 16,000 daltons.
