Linked Life Data

7059599

Source:http://linkedlifedata.com/resource/pubmed/id/7059599

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1982-5-21
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
685
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
177-81
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Immunoglobulin-lipid interaction. A model membrane study.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't