Properties of monoacylglycerol lipase in rabbit aorta.
Monacylglycerol lipase activity was characterized in a soluble preparation from rabbit aorta (intima-media) obtained by combining a 100,000 x g supernatant fraction with activity solubilized from the 100,000 x 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 microM) 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.
Hee-Cheong
M
M
Department of Pharmacology and Therapeutics, Faculty of Medicine, University of Calgary, Alberta, Canada.
Severson
D L
DL
D000818:Animals; D001011:Aorta / Q000201:enzymology*; D002122:Calcium Chloride / Q000494:pharmacology; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D007700:Kinetics; D008994:Monoacylglycerol Lipases / Q000302:isolation & purification / Q000378:metabolism*; D009131:Muscle, Smooth, Vascular / Q000201:enzymology; D009994:Osmolar Concentration; D011817:Rabbits; D012965:Sodium Chloride / Q000494:pharmacology; D012969:Sodium Fluoride / Q000494:pharmacology; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity
D012965:Sodium Chloride; D012969:Sodium Fluoride; D002265:Carboxylic Ester Hydrolases; D008994:Monoacylglycerol Lipases; D002122:Calcium Chloride