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冷凝集素之间的交叉独特型特异性与血型相关抗原的结合活性的关系。

Cross idiotypic specificity among cold agglutinins in relation to combining activity for blood group-related antigens.

作者信息

Feizi T, Kunkel H G, Roelcke D

出版信息

Clin Exp Immunol. 1974 Oct;18(2):283-93.

PMID:4468199
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1537898/
Abstract

The previous observations of cross idiotypic specificity of IgM cold agglutinins were further investigated in quantitative precipitin assays and attempts were made to relate shared idiotypic specificity to combining specificity for I, i and Pr antigens of red cells. Shared idiotypic determinants were observed among anti-I and anti-i antibodies which are now known to have combining specificity for determinants present on precursors of the ABH and Lewis blood group substances. There was evidence that one cold agglutinin, Ma, which had previously been shown to have an unusual kind of I specificity was deficient in the idiotypic determinants associated with the other anti-I proteins. Anti-Pr cold agglutinins, which have specificities unrelated to I-i antigens, were found to have distinct cross idiotypic determinants which were not detected on anti-I and anti-i antibodies. IgA and IgM antibodies with Pr specificity isolated from different individuals were found to share idiotypic determinants. Cross specificity antigens were detected at low concentrations in preparations of normal IgG and IgM, but not in any isolated monoclonal macroglobulins lacking cold agglutinin activity.

摘要

在定量沉淀试验中,对先前关于IgM冷凝集素交叉独特型特异性的观察结果进行了进一步研究,并尝试将共享的独特型特异性与对红细胞I、i和Pr抗原的结合特异性联系起来。在抗I和抗i抗体之间观察到共享的独特型决定簇,现在已知这些抗体对ABH和Lewis血型物质前体上存在的决定簇具有结合特异性。有证据表明,一种冷凝集素Ma,以前被证明具有一种不寻常的I特异性,缺乏与其他抗I蛋白相关的独特型决定簇。抗Pr冷凝集素的特异性与I-i抗原无关,被发现具有独特的交叉独特型决定簇,而在抗I和抗i抗体上未检测到这些决定簇。从不同个体分离出的具有Pr特异性的IgA和IgM抗体被发现共享独特型决定簇。在正常IgG和IgM制剂中检测到低浓度的交叉特异性抗原,但在任何缺乏冷凝集素活性的分离单克隆巨球蛋白中均未检测到。

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Cross idiotypic specificity among cold agglutinins in relation to combining activity for blood group-related antigens.冷凝集素之间的交叉独特型特异性与血型相关抗原的结合活性的关系。
Clin Exp Immunol. 1974 Oct;18(2):283-93.
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