人类风湿因子交叉独特型。I. WA和BLA是热不稳定的构象抗原，重链和轻链均不可或缺。
Human rheumatoid factor crossidiotypes. I. WA and BLA are heat-labile conformational antigens requiring both heavy and light chains.
作者信息
Agnello V, Barnes J L
出版信息
J Exp Med. 1986 Nov 1;164(5):1809-14. doi: 10.1084/jem.164.5.1809.
Abstract
Evidence was obtained that both the WA and BLA crossidiotype (XId) groups are conformational antigens requiring both L and H chains and that with heat denaturation the antigens that define the XIds and antigen-binding activity are lost in parallel. In contrast, the primary structure-dependent crossreactive idiotype (CRI), PSL2, which is only weakly detected on native Wa and Bla monoclonal rheumatoid factors (mRFs), became prominently detected on the heated Wa and Bla mRFs. Heat denaturation may provide a simple method for distinguishing Ids determined by conformational antigen from primary structure-dependent Ids. In addition to heat denaturation, some acid conditions commonly used for preparation of RFs were also found to cause marked loss of Id antigen. The finding of PSL2-CRI on Bla mRF indicates that this Id is not unique to the WA XId.
摘要
有证据表明，WA和BLA交叉独特型（XId）组都是需要轻链和重链的构象抗原，并且随着热变性，定义XIds的抗原和抗原结合活性会同时丧失。相比之下，主要结构依赖性交叉反应独特型（CRI）PSL2在天然的Wa和Bla单克隆类风湿因子（mRFs）上仅能微弱检测到，但在加热后的Wa和Bla mRFs上则能显著检测到。热变性可能提供一种简单的方法，用于区分由构象抗原决定的独特型和主要结构依赖性独特型。除了热变性外，还发现一些常用于制备RFs的酸性条件也会导致独特型抗原显著丧失。在Bla mRF上发现PSL2-CRI表明，这种独特型并非WA XId所特有。
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Similarities in the light chains of anti-gamma-globulins showing cross-idiotypic specificities.显示交叉独特型特异性的抗γ球蛋白轻链中的相似性。
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