Abstract
Monoacylglycerol lipase activity was characterized in a soluble preparation from rabbit aorta (intima-media) obtained by combining a 100,000×g supernatant fraction with activity solubilized from the 100,000×g precipitate fraction by treatment with Triton X-100. Rates of hydrolysis with 1-monoolein and 2-monoolein substrates were nearly identical. 1-Monoolein was a competitive inhibitor (Ki 65 μM) of 2-monoolein hydrolysis. 2-Monoolein and 2-monopalmitin were both hydrolyzed more rapidly than 2-monoarachidonin. Lipase activity measured with a 2-monoolein substrate was inhibited by the addition of oleate, NaF and CaCl2 to the assay. Preincubation of the lipase preparation with p-bromophenacyl bromide resulted in a potent inhibition of lipase activity; this inhibition could be prevented by dithiothreitol.
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Abbreviations
- DG:
-
diacylglycerol
- 2-MG:
-
2-monoacylglycerol
- DTT:
-
dithiothreitol
- TLC:
-
thin layer chromatography
- BPB:
-
p-bromophenacyl bromide
- PMSF:
-
phenylmethylsulfonyl fluoride
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Hee-Cheong, M., Severson, D.L. Properties of monoacylglycerol lipase in rabbit aorta. Lipids 22, 999–1004 (1987). https://doi.org/10.1007/BF02536439
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DOI: https://doi.org/10.1007/BF02536439