Influence of ethanol and phosphatidylethanol on the activity of pancreatic phospholipase A2.
Hydrolysis of dioleoylphosphatidylethanol (DOPEt) and dioleoylphosphatidylcholine (DOPC) catalyzed by phospholipase A2 (PLA2) from porcine pancreas has been studied in single-component and binary liposomes in the absence and in the presence of ethanol. DOPEt (an anionic phospholipid) was found to increase the rate of hydrolysis of zwitterionic DOPC in liposomes under the action of PLA2.
Kisel
M A
MA
Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, Minsk, 220141, Belarus. kisel@ns.iboch.ac.by
Kuchuro
S V
SV
Litvinko
N M
NM
D000818:Animals; D002151:Calorimetry; D004789:Enzyme Activation; D000431:Ethanol / Q000494:pharmacology*; D020404:Glycerophospholipids / Q000494:pharmacology*; D006868:Hydrolysis; D007700:Kinetics; D010179:Pancreas / Q000187:drug effects* / Q000201:enzymology; D010713:Phosphatidylcholines / Q000378:metabolism; D010741:Phospholipases A / Q000378:metabolism*; D054467:Phospholipases A2; D013552:Swine
D020404:Glycerophospholipids; D010713:Phosphatidylcholines; C051521:phosphatidylethanol; D000431:Ethanol; D010741:Phospholipases A; D054467:Phospholipases A2; C017251:1,2-oleoylphosphatidylcholine