Abstract
Lipoprotein lipase (LPL) is an N-inked glycoprotein of approximately 57 kDa that is synthesized by a numbel of tissues, including white and brown adipose tissue, heart, skeletal muscle, neonatal liver and brain (1,2). In these tissues, LPL is synthesized by parenchymal cells and secreted to the surface of endothelial cells where it is bound by heparan sulfate proteoglycans. Endothelial-bound LPL hydrolyzes triglycerides from the core lipids of chylomicrons and very low density lipoproteins, liberating free fatty acids that can be utilized by the subjacent tissue for storage or oxidation.
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© 1999 Humana Press Inc, Totowa, NJ
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Doolittle, M.H., Ben-Zeev, O. (1999). Immunodetection of Lipoprotein Lipase: Antibody Production, Immunoprecipitation, and Western Blotting Techniques. In: Doolittle, M., Reue, K. (eds) Lipase and Phospholipase Protocols. Methods in Molecular Biology™, vol 109. Humana Press. https://doi.org/10.1385/1-59259-581-2:215
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DOI: https://doi.org/10.1385/1-59259-581-2:215
Publisher Name: Humana Press
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