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 Citations (Scopus)

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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Phosphatidylcholine-Sterol O-Acyltransferase
Phospholipases A2
Human Activities
Pressure
Phospholipases
Phosphatidylcholines
Lipoproteins
Monolayers
Enzymes

Cite this

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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 journalArticle

TY - JOUR

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