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 26-28 mN/m. These data suggest that lipoprotein surface pressure may regulate lecithin-cholesterol acyltransferase activity in vivo.
Original language | English |
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Pages (from-to) | 840-846 |
Number of pages | 7 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 211 |
Issue number | 3 |
DOIs | |
State | Published - 1 Jan 1995 |