Effect of apolipoprotein C-II on the lipoprotein lipase-catalyzed hydrolysis of dihexanoyl- and diheptanoyl-phosphatidylcholine.
The effect of apolipoprotein C-II (apoC-II) on the lipoprotein lipase (LpL)-catalyzed hydrolysis of phospholipids was studied using purified bovine milk LpL and dihexanoyl (diC6) and diheptanoyl (diC7) phosphatidylcholine. In contrast to porcine pancreatic phospholipase A2, the LpL-catalyzed hydrolysis of these short-chain lecithins was not enhanced at substrate concentrations above the critical micelle concentration of the lipids. Furthermore, apoC-II had no effect on enzyme catalysis.
D000818:Animals; D053304:Apolipoprotein C-II; D001053:Apolipoproteins / Q000494:pharmacology*; D001056:Apolipoproteins C; D002384:Catalysis; D002417:Cattle; D004789:Enzyme Activation / Q000187:drug effects; D006868:Hydrolysis; D008071:Lipoprotein Lipase / Q000378:metabolism*; D008823:Micelles; D008892:Milk / Q000201:enzymology; D010713:Phosphatidylcholines / Q000378:metabolism*; D013379:Substrate Specificity
D053304:Apolipoprotein C-II; D001053:Apolipoproteins; D001056:Apolipoproteins C; D008823:Micelles; D010713:Phosphatidylcholines; C038470:1,2-heptanoylphosphatidylcholine; C032166:1,2-hexanoylphosphatidylcholine; D008071:Lipoprotein Lipase