Immunological relevance of malonic dialdehyde (MDA): III. Immuno-enzymatic determination of human immunoglobulin binding to MDA-crosslinked proteins.
Using immunoenzymatic reactions (ELISA) with MDA-crosslinked lysozyme (ML) or poly-L-lysine (MP) and with the corresponding native protein or polypeptide, we showed that sera from normal human subjects contain immunoglobulins with antibody-like specificity for MDA-modified proteins. Inhibition studies with ML and MP showed that the chemical structures recognized by these immunoglobulins include 1-amino-3-iminopropene (AIP) bridges resulting from reactions of MDA with primary amino groups. An ELISA technique for quantitation of these immunoglobulins was developed and applied to 32 sera from healthy humans, which provided an estimation of their normal levels. Variations of these levels under pathological conditions are now being investigated.
Kergonou
J F
JF
Centre de Recherches du Service de Santé des Armées, Clamart, France.
Pennacino
I
I
Lafite
C
C
Ducousso
R
R
D003432:Cross-Linking Reagents; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D007136:Immunoglobulins / Q000378:metabolism*; D008314:Malonates / Q000276:immunology*; D008315:Malondialdehyde / Q000276:immunology*; D009113:Muramidase / Q000276:immunology; D011107:Polylysine; D011485:Protein Binding
D003432:Cross-Linking Reagents; D007136:Immunoglobulins; D008314:Malonates; D011107:Polylysine; D008315:Malondialdehyde; D009113:Muramidase