Effect of interfacial pressure on the binding and phospholipase A2 activity of recombinant human lecithin-cholesterol acyltransferase

Richard B. Weinberg; Jennifer B. Jones; P. Haydn Pritchard; Andras G. Lacko

doi:10.1006/bbrc.1995.1888

Effect of interfacial pressure on the binding and phospholipase A2 activity of recombinant human lecithin-cholesterol acyltransferase

Richard B. Weinberg, Jennifer B. Jones, P. Haydn Pritchard, Andras G. Lacko

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

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	https://doi.org/10.1006/bbrc.1995.1888
State	Published - 1 Jan 1995

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10.1006/bbrc.1995.1888

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title = "Effect of interfacial pressure on the binding and phospholipase A2 activity of recombinant human lecithin-cholesterol acyltransferase",

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.",

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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. et al.

In: Biochemical and Biophysical Research Communications, Vol. 211, No. 3, 01.01.1995, p. 840-846.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Effect of interfacial pressure on the binding and phospholipase A2 activity of recombinant human lecithin-cholesterol acyltransferase

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AU - Jones, Jennifer B.

AU - Haydn Pritchard, P.

AU - Lacko, Andras G.

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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.

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DO - 10.1006/bbrc.1995.1888

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ER -

Effect of interfacial pressure on the binding and phospholipase A2 activity of recombinant human lecithin-cholesterol acyltransferase

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