Abstract
We examined the effect of surface pressure on the interfacial binding and phospholipase A2 activity of lecithin-cholesterol acyltransferase. The enzyme bound to phosphatidylcholine monolayers with an apparent dissociation constant of 1.5 nM was excluded from the interface at pressures > 29 mN/m and exhibited maximal phospholipase activity at pressures between 29-28 mN/m. These data suggest that lipoprotein surface pressure may regulate lecithin-cholesterol acyltransferase activity in vivo.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Humans
-
Hydrolysis
-
Hydrostatic Pressure
-
Membranes, Artificial
-
Phosphatidylcholine-Sterol O-Acyltransferase / metabolism*
-
Phosphatidylcholines / metabolism
-
Phospholipases A / metabolism*
-
Phospholipases A2
-
Recombinant Proteins / metabolism
-
Surface Properties
Substances
-
Membranes, Artificial
-
Phosphatidylcholines
-
Recombinant Proteins
-
Phosphatidylcholine-Sterol O-Acyltransferase
-
Phospholipases A
-
Phospholipases A2