Membrane insertion and antibody recognition of a glycosylphosphatidylinositol-anchored protein: an optical study.

Détails

ID Serval
serval:BIB_EFC76C5E887D
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Membrane insertion and antibody recognition of a glycosylphosphatidylinositol-anchored protein: an optical study.
Périodique
Biochemistry
Auteur(s)
Ramsden J.J., Schneider P.
ISSN
0006-2960 (Print)
ISSN-L
0006-2960
Statut éditorial
Publié
Date de publication
1993
Volume
32
Numéro
2
Pages
523-529
Langue
anglais
Résumé
The kinetics of binding of a glycolipid-anchored protein (the promastigote surface protease, PSP) to planar lecithin bilayers is studied by an integrated optics technique, in which the bilayer membrane is supported on an optical wave guide and the phase velocities of guided light modes in the wave guide are measured. From these velocities, the optical parameters of the membrane and PSP layers deposited on the waveguide are determined, yielding in particular the mass of PSP bound to the membrane, which is followed in real time. From a comparison of the binding rates of PSP and PSP from which the lipid moiety has been removed, it is shown that the lipid moiety plays a key role in anchoring the protein to the membrane. Specific and nonspecific binding of antibodies to membrane-anchored PSP is also investigated. As little as a fifth of a monolayer of PSP is sufficient to suppress the appreciable nonspecific binding of antibodies to the membrane.
Mots-clé
Animals, Antibodies, Protozoan/immunology, Glycosylphosphatidylinositols/immunology, Glycosylphosphatidylinositols/metabolism, Kinetics, Leishmania/immunology, Leishmania/metabolism, Lipid Bilayers, Membrane Proteins/immunology, Membrane Proteins/metabolism, Metalloendopeptidases/immunology, Metalloendopeptidases/metabolism, Optics and Photonics
Pubmed
Web of science
Création de la notice
19/01/2008 18:31
Dernière modification de la notice
03/03/2018 22:35
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