Adsorption of a phospholipid-hydroperoxide glutathione peroxidase into phospholipid monolayers at the air-water interface

S Morandat, M Bortolato, Fergus Nicol, John Arthur, J P Chauvet, B Roux

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5 Citations (Scopus)


The interfacial behavior differences of two glutathione peroxidase isoforms have been investigated. The first isoform is the phospholipid-hydroperoxide glutathione peroxidase (EC (GPx-4) isolated from rat testes and the second one is the cytosolic glutathione peroxidase (EC 1.11. 1.9) (GPx-1) from bovine erythrocytes. Injected in the subphase buffer of a Langmuir trough, GPx-4 was able to adsorb quickly at the air-water interface whereas the GPx-1 was not. Then, the protein interaction with phospholipid monolayers was explored. Indeed, a monolayer of phospholipids containing a different number of polyunsaturated fatty acyl chains was prepared at the air-water interface. Under each kind of monolayer, the protein solution was injected and its adsorption was visualized by the measurement of successive pressure-area isotherms. We have, then, determined the molecular area increase due to the protein adsorption. It was found that the GPx-4 is adsorbed in each kind of monolayer tested whereas no molecular area increase was detected with the GPx-1. This indicates that the GPx-4 has a higher affinity for the interface, recovered or not by lipids, than the GPx-1. Moreover, the GPx-4 presents a different affinity for the phospholipid monolayers depending on the number of polyunsaturated fatty acyl chains. (C) 2004 Elsevier B.V. All rights reserved.

Original languageEnglish
Pages (from-to)99-105
Number of pages7
JournalColloids and Surfaces. B, Biointerfaces
Issue number2
Publication statusPublished - 15 May 2004


  • glutathione peroxidase
  • protein adsorption
  • protein-lipid interactions
  • Langmuir monolayer
  • polyunsaturated phospholipids
  • bovine serum-albumin
  • air/water interface
  • beta-lactoglobulin
  • mixed monolayers
  • membranes
  • purification
  • lipids


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