Effect of Hydrostatic Pressure on the Transfer of a Fluorescent Phosphatidylcholine between Apolipoprotein-Phospholipid Recombinants

William W. Mantulin, Antonio Gotto, Henry J. Pownall

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

The effect of high hydrostatic pressure on the mechanism of transfer for lipophiles between membranes was investigated. The transfer of fluorescent phosphatidylcholine (1-myristoyl-2- left bracket 9 prime -(3 prime -pyrenyl)nonanoyl right bracket phosphatidylcholine) between recombinant complexes of apolipoprotein A-I and 1-palimitoyl-2-oleoylphosphatidylcholine occurred via the aqueous compartment. High hydrostatic pressure retarded the rate of transfer, resulting in a positive activation volume for the reaction. The calculated free energy of activation was approximately 23 kcal/mol. The positive activation volume presumably corresponds to the work necessary to overcome pressure-induced compression of the membrane (protein-lipid complex) before transfer can occur.

Original languageEnglish (US)
Pages (from-to)3317-3319
Number of pages3
JournalJournal of the American Chemical Society
Volume106
Issue number11
DOIs
StatePublished - Jan 1 1984

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Fingerprint Dive into the research topics of 'Effect of Hydrostatic Pressure on the Transfer of a Fluorescent Phosphatidylcholine between Apolipoprotein-Phospholipid Recombinants'. Together they form a unique fingerprint.

Cite this