Contribution of the H- and L-chains and of the binding site to the idiotypic specificities of mouse anti-GAT antibodies.
Contribution of the H- and L-chains and of the binding site to the idiotypic specificities of mouse anti-GAT antibodies.
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H 链和 L 链以及结合位点对小鼠抗 GAT 抗体独特型特异性的贡献。
DOI：
10.1016/0161-5890(82)90309-1
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发表时间：
1982
影响因子：
3.6
通讯作者：
B. O. To
中科院分区：
文献类型：
--
作者：
G. Sommé;JoséRocca Serra;Lise Leclercq;Jean;E. Mazie;D. Moinier;M. Fougereau;D. J. Theze;B. O. To
研究了H链和l链对抗聚（Glu60-Ala30Tyr10） （GAT）抗体主要独特型结构的贡献。这种独特型以前被分为四种类型的特异性：(1)高度保守的独特型特异性（h.c.GAT）由来自豚鼠、大鼠和小鼠的抗gat抗体表达；(2)公共特异性（p.GAT）由所有被试小鼠品系的所有抗gat抗体和所有具有抗gat活性的杂交瘤产物（HP）以相同的形式表达；(3)菌株限制性特异性（srgat -1）仅由具有Ig-1a、ig - ici和ig - ieallotype标记的菌株的抗gat抗体表达；最后(4)个体特异性，HP G5上定义的- gatj也被大多数具有抗聚（Glu50Tyr50） （GT）活性的杂交瘤蛋白表达。在本文中，我们证明了。gatandij - gate需要H-链和l -链相互作用才能表达：(1)HP G5分离的H-链和l -链不表达这些特异性；(2)具有抗gat活性的HP的H链和l链组成的重组分子和无关的骨髓瘤蛋白（MOPC21）从未表达。GATandij-GAT，我们进一步研究了GAT结合位点与p.GAT.h.c. gatands .r之间的关系。GAT-1独特型特异性。GAT和GT均不能抑制与。r的结合。GAT-1，同时抑制独特型结合顶部。mol. wt 3000的GAT片段也被证明可以抑制p. gatand h.c. gatto与相应血清的结合。因此，.GAT和. c.g at非常接近GAT结合位点，而.r。GAT-1表现出位于GAT结合位点外的独特型特异性。
The contribution of the H- and L-chains to the structure of the main idiotype of anti-poly (Glu60-Ala30Tyr10) (GAT) antibodies has been studied. This idiotype has been previously divided into four types of specificity: (1) the highly conserved idiotypic specificity (h.c.GAT) is expressed by anti-GAT antibodies from the guinea-pig, rat and mice; (2) the public specificity (p.GAT) is expressed in an identical form by all anti-GAT antibodies from all strains of mice tested and by all hybridoma products (HP) with anti-GAT activity; (3) the strain-restricted specificity (s.r.GAT-1) is only expressed by anti-GAT antibodies from strains with Ig-1a, Ig-Icand Ig-Ieallotypic markers; and finally (4) the individual specificityij,-GATdefined on HP G5 is also expressed by most of the hybridoma protein with anti-poly (Glu50Tyr50) (GT) activity.In this paper we-show thath.c.GAT,p.GATandij-GATrequire the interaction of H- and L-chains to be expressed: (1) isolated H- and L-chains from HP G5 did not express these specificities; and (2) recombinant molecules composed of H- and L-chains from HP with anti-GAT activity and an irrelevant myeloma protein (MOPC21) never expressedh.c.GAT,p.GATandij-GAT,We next investigated the relationship between the GAT binding site and thep.GAT.h.c.GATands.r.GAT-1 idiotypic specificities. GAT and GT were not able to inhibit the binding tos.r.GAT-1 while they inhibit the idiotypic binding top.GATandh.c.GAT. A GAT fragment of mol. wt 3000 was also shown to inhibit the binding ofp.GATandh.c.GATto the appropriate sera. Thusp.GATandh.c.GATare very close to the GAT combining site whiles.r.GAT-1 represents an idiotypic specificity located outside the GAT binding site.