Kergonou J F, Pennacino I, Lafite C, Ducousso R
Centre de Recherches du Service de Santé des Armées, Clamart, France.
Biochem Int. 1988 May;16(5):835-43.
Using precipitation reactions in agarose gels (Bidimensional double diffusion: Ouchterlony. Counterimmunoelectrophoresis: CEP), we showed that: a) sera from normal human subjects contain components able to bind and precipitate with MDA-crosslinked lysozyme (ML) and not with native lysozyme, which indicates that the chemical structures involved in such bindings arise from reaction of MDA with lysozyme and probably include 1-amino-3-iminopropene (AIP) bridges. b) some if not all of these seric components are immunoglobulins. c) the F(ab')2 regions of these immunoglobulins are involved in their binding and precipitating properties. These results lead us to assume that sera from normal human subjects contain immunoglobulins with antibody-like specificity for MDA-crosslinked proteins. Nevertheless, this assumption remains to be assessed by further studies, especially about the "epitopes" involved in such reactions.
利用琼脂糖凝胶中的沉淀反应（双向双扩散：奥克特洛尼法。对流免疫电泳：CEP），我们发现：a）正常人血清中含有能够与丙二醛交联溶菌酶（ML）结合并沉淀，而不与天然溶菌酶结合并沉淀的成分，这表明参与此类结合的化学结构源自丙二醛与溶菌酶的反应，可能包括1-氨基-3-亚氨基丙烯（AIP）桥。b）这些血清成分中即便不是全部，也有一些是免疫球蛋白。c）这些免疫球蛋白的F(ab')2区域参与其结合和沉淀特性。这些结果使我们推测，正常人血清中含有对丙二醛交联蛋白具有抗体样特异性的免疫球蛋白。然而，这一推测仍有待进一步研究评估，尤其是关于此类反应中涉及的“表位”。
