Lipoprotein lipase in rat heart--I. Characterization of tri-, di- and monoacylglycerol lipase activities in post-heparin effluents.
1. The lipolytic activities that sequentially hydrolyze tri-, di- and monoacylglycerol in rat post-heparin heart effluents were examined. 2. Properties of triacylglycerol lipase (TAGL) activity were typical of lipoprotein lipase. Diacylglycerol lipase (DAGL) behaved similarly to TAGL, suggesting that both activities refer to the same catalytic entity. 3. Differences, particularly in thermal stability, between TAGL and DAGL activities on one hand, and monoacylglycerol lipase (MAGL) activity on the other, may reflect different intrinsic molecular properties. 4. TAGL, DAGL and MAGL activities could not be separated by physical means and appeared to belong to a single unit at the same site on the capillary wall.
Benkirane
M
M
INSERM U.260, Faculté de Médecine, Marseille, France.
Meignen
J M
JM
Boyer
J
J
Verine
A
A
D000818:Animals; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D004075:Diglycerides / Q000378:metabolism; D005260:Female; D006493:Heparin / Q000494:pharmacology; D007700:Kinetics; D008071:Lipoprotein Lipase / Q000378:metabolism*; D008994:Monoacylglycerol Lipases / Q000378:metabolism*; D009206:Myocardium / Q000201:enzymology*; D009829:Oleic Acids / Q000494:pharmacology; D010477:Perfusion; D051381:Rats; D011919:Rats, Inbred Strains; D013696:Temperature
D004075:Diglycerides; D009829:Oleic Acids; D006493:Heparin; D002265:Carboxylic Ester Hydrolases; D008994:Monoacylglycerol Lipases; D008071:Lipoprotein Lipase