par Vandenbranden, Michel 
;Kayser, G;Banerjee, Sunanda ;Ruysschaert, Jean Marie
Référence Biochimica et biophysica acta, 685, 2, page (177-181)
Publication Publié, 1982-02
;Kayser, G;Banerjee, Sunanda ;Ruysschaert, Jean Marie Référence Biochimica et biophysica acta, 685, 2, page (177-181)
Publication Publié, 1982-02
Article révisé par les pairs
| Résumé : | We recently presented evidence (Vandenbranden, M., De Coen, J.L., Jeener, R., Kanarek, L. and Ruysschaert, J.M. (1981) Mol. Immunol. 8, 621-631) for the existence of two conformational rabbit serum IgG immunoglobulin isomers. In the present report, their capacity to interact with lipid is investigated in model membranes. (1) One isomer, IgG(H), behaves like several intrinsic membrane proteins: it induces a large surface pressure increase when injected under a lipid monolayer in the close packed state and increases by 20-fold the conductance of a planar bilayer. The other isomer, IgG(S) doesn't interact significantly with the lipids. (2) IgG(H) marked a preference for monolayers made of lipids with a negatively charged polar headgroup and bearing unsaturations in their acyl chains. Penetration is stronger with lipid monolayer in the fluid state than in the rigid state. (3) As previously shown (Vanderbranden, M., De Coen, J.L., Jeener, R., Kanarek, L. and Ruysschaert, J.M. (1918) Mol. Immunol. 18, 621-631), circular dichroïsm spectra and antigen precipitation tests don't allow to detect any difference in the overall secondary conformation and antigen recognition properties of the two isomers. (4) Papaïn cleavage of the hinge region suppresses the hydrophobic properties of IgG towards lipid monolayers. (5) The hypothesis of a binding of the hinge region with the lipid bilayer is discussed. |
