Abstract
A rapid assay for lipoprotein lipase activity employing a (14)C-labeled substrate is described. The method is very sensitive and suitable for routine use.
Highlights
Since more than one lipase is usually present in crude extracts from adipose tissue it is difficult, if not impossible, to determine what part of the enzyme activity measured by the appearance of fatty acid is derived from the mono, di, or triglyceride contained in the Ediol
Greten, Levy, and Fredrickson (4)have described an assay for lipoprotein lipase activity in which a pure radioactive triglyceride is used
The reaction was terminated by addition of 4 ml of isopropanol-3 N H 2 S 0 440: 1. For the extraction of the lipids, 2 ml of HzO and 5 ml of hexane were added (6), and the tube was shaken end-toend on a mechanical shaker for 1 min. 20 rnin later a 5 ml aliquot of the hexane phase was added to 1 nil 0.1 N KOH
Summary
This enzyme has been extensively studied for a number of years, a recurring problem has been the choice of a substrate for measuring its activity. Since more than one lipase is usually present in crude extracts from adipose tissue it is difficult, if not impossible, to determine what part of the enzyme activity measured by the appearance of fatty acid is derived from the mono-, di-, or triglyceride contained in the Ediol. Greten, Levy, and Fredrickson (4)have described an assay for lipoprotein lipase activity in which a pure radioactive triglyceride is used.
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