Highly purified rat hepatic lipase (NaCl-resistant, alkaline pH optimum) was studied to evaluate whether the enzyme has triacylglycerol lipase, monoacylglycerol lipase and phospholipase activities. Enzyme exhibiting a single band by SDS-polyacrylamide gel electrophoresis and having a specific activity eight times greater than that in any previous report was utilized. The ratios of the different lipolytic activities to each other remained constant throughout a multistep hepatic lipase purification. The lipolytic activities coeluted by gel filtration on Ultrogel AcA 34. Column isoelectric focusing of the highly purified enzyme revealed comigration of the lipolytic activities. Thermal inactivation produced similar decay curves for the different activities. Immune titration curves for the different activities with specific antibody against hepatic lipase were essentially identical. These findings indicate that hepatic lipase is a single enzyme molecule which has triacylglycerol lipase, monoacylglycerol lipase and phospholipase activities with artificial substrates. To study these lipolytic activities further, highly purified hepatic lipase was subjected to limited digestion by specific proteases. The triacylglycerol lipase activity was more sensitive to proteolytic destruction than either of the other two activities.
|Original language||English (US)|
|Number of pages||7|
|Journal||Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism|
|State||Published - Mar 12 1982|
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