Hydrolysis of phosphatidylcholine by phospholipase A2 does not cause dissociation of apolipoprotein C from rat plasma very low density lipoprotein.
To test the hypothesis that hydrolysis of glycerophosphatides causes displacement of apolipoprotein C from very low density lipoprotein, we have studied the effects of a snake venom phospholipase A2 on very low density lipoprotein labeled with [125I]apoC, [3H]cholesterol, [14C]palmitate and [32P]phospholipids. In spite of hydrolysis of 97% of the phosphatidylcholine, only small amounts of labeled apoC and labeled cholesterol were displaced from the very low density lipoprotein. With purified lipoprotein lipase in contrast, 80-90% of the labeled apoC and cholesterol were removed from the lipoprotein. It is concluded that hydrolysis of phosphatidylcholine does not cause an appreciable dissociation of apolipoprotein C from very low density lipoprotein.
D000818:Animals; D001053:Apolipoproteins / Q000097:blood*; D002784:Cholesterol / Q000032:analysis; D008079:Lipoproteins, VLDL / Q000097:blood*; D008297:Male; D010169:Palmitic Acids / Q000032:analysis; D010713:Phosphatidylcholines / Q000097:blood; D010740:Phospholipases; D010743:Phospholipids / Q000032:analysis; D051381:Rats
D001053:Apolipoproteins; D008079:Lipoproteins, VLDL; D010169:Palmitic Acids; D010713:Phosphatidylcholines; D010743:Phospholipids; D002784:Cholesterol; D010740:Phospholipases