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

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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
Publication status	Published - 1 Jan 1995

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Weinberg, R. B., Jones, J. B., Haydn Pritchard, P., & Lacko, A. G. (1995). Effect of interfacial pressure on the binding and phospholipase A2 activity of recombinant human lecithin-cholesterol acyltransferase. Biochemical and Biophysical Research Communications, 211(3), 840-846. https://doi.org/10.1006/bbrc.1995.1888

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10.1006/bbrc.1995.1888

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