Vlasov V V, Pautova L V, Rykova E Iu, Iakubov L A
Biokhimiia. 1993 Aug;58(8):1247-51.
The interaction of alkylating derivatives of deoxyribonucleotides whose 5'-terminal phosphate group contains a 4-[(N-2-chloroethyl-N-methyl)amino]benzylamine residue with serum proteins has been studied. Incubation of whole human sera with various concentrations of the alkylating derivative, p(T)16, resulted in affinity modification of several proteins, among which albumin as well as IgM and IgG were the most readily detectable ones. The type of dependence of the degree of modification of these proteins on oligonucleotide concentration suggests that the oligonucleotides display a higher affinity for IgM than for IgG and albumin. Binding of reactive oligomer derivatives to serum proteins was inhibited by polyanions of different oligomeric composition, two-chain DNA and heparin, the latter being the strongest inhibitor of the immunoglobulins. These data point to a role of nonspecific ion-to-ion interactions in the IgG-oligonucleotide complex formation. Oligonucleotide interaction with murine monoclonal antibodies GI was inhibited by a specific antigen which suggests that oligonucleotides may interact with immunoglobulin either at or near a site where the antigen is recognized by the antibody.
对5'-末端磷酸基团含有4-[(N-2-氯乙基-N-甲基)氨基]苄胺残基的脱氧核糖核苷酸烷基化衍生物与血清蛋白之间的相互作用进行了研究。将全人血清与不同浓度的烷基化衍生物p(T)16一起孵育，导致几种蛋白质发生亲和修饰，其中白蛋白以及IgM和IgG是最容易检测到的。这些蛋白质的修饰程度对寡核苷酸浓度的依赖类型表明，寡核苷酸对IgM的亲和力高于对IgG和白蛋白的亲和力。不同寡聚组成的聚阴离子、双链DNA和肝素可抑制反应性寡聚物衍生物与血清蛋白的结合，肝素是免疫球蛋白最强的抑制剂。这些数据表明非特异性离子间相互作用在IgG-寡核苷酸复合物形成中起作用。寡核苷酸与鼠单克隆抗体GI的相互作用受到特异性抗原的抑制，这表明寡核苷酸可能在抗体识别抗原的位点处或附近与免疫球蛋白相互作用。
