Preparation of a Homogenous and Stable form of Bovine Milk Lipoprotein Lipase |
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| Authors: | L. Socorro C. C. Green R. L. Jackson |
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| Affiliation: | 1. Division of Lipoprotein Research Department of Pharmacology and Cell Biophysics and Department of Biochemistry and Molecular Biology , University of Cincinnati College of Medicine , Cincinnati, Ohio, 45267-0575;2. Merrell Dow Research Institute , Cincinnati, Ohio, 45215 |
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| Abstract: | 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. |
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