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 journalArticle

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 languageEnglish
Pages (from-to)840-846
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume211
Issue number3
DOIs
StatePublished - 1 Jan 1995

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