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 |
|---|---|
| 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 |
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Effect of interfacial pressure on the binding and phospholipase A2 activity of recombinant human lecithin-cholesterol acyltransferase. / Weinberg, Richard B.; Jones, Jennifer B.; Haydn Pritchard, P.; Lacko, Andras G.
In: Biochemical and Biophysical Research Communications, Vol. 211, No. 3, 01.01.1995, p. 840-846.Research output: Contribution to journal › Article
TY - JOUR
T1 - Effect of interfacial pressure on the binding and phospholipase A2 activity of recombinant human lecithin-cholesterol acyltransferase
AU - Weinberg, Richard B.
AU - Jones, Jennifer B.
AU - Haydn Pritchard, P.
AU - Lacko, Andras G.
PY - 1995/1/1
Y1 - 1995/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0029017707&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1995.1888
DO - 10.1006/bbrc.1995.1888
M3 - Article
C2 - 7598713
AN - SCOPUS:0029017707
VL - 211
SP - 840
EP - 846
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -