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.