SEGMENTAL FLEXIBILITY AND COMPLEMENT-FIXATION OF GENETICALLY ENGINEERED CHIMERIC HUMAN, RABBIT AND MOUSE ANTIBODIES
SEGMENTAL FLEXIBILITY AND COMPLEMENT-FIXATION OF GENETICALLY ENGINEERED CHIMERIC HUMAN, RABBIT AND MOUSE ANTIBODIES
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DOI：
10.1002/j.1460-2075.1988.tb03037.x
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发表时间：
1988-07-01
期刊：
影响因子：
11.4
通讯作者：
OI, VT
中科院分区：
文献类型：
--
作者：
DANGL, JL;WENSEL, TG;OI, VT
我们产生了一个嵌合免疫球蛋白G(IgG)分子家族，该分子具有与Dansyl(DNS)半抗原相同的抗原结合部位，以及9个重链常数(CH)区域。这一抗体分子家族允许比较CH依赖的性质，而不依赖于可能的可变区对免疫球蛋白功能的贡献。用体细胞遗传学技术测定了6个基因工程分子(4个人免疫球蛋白亚型、小鼠免疫球蛋白G3和兔免疫球蛋白)和3个小鼠免疫球蛋白亚型(IgG1、IgG2a和IgG2b)的片段柔韧性和补体结合活性。抗体分子的这些性质都与免疫球蛋白铰链区的长度相关，免疫球蛋白铰链区分隔第一和第二个CH(CH1和CH2)结构域。这些结果为抗体分子的两个关键性质提供了结构基础。
We generated a family of chimeric immunoglobulin G (IgG) molecules having identical antigen-combining sites for the dansyl (DNS) hapten, in conjunction with nine heavy chain constant (CH) regions. This family of antibody molecules allows comparison of CH dependent properties independent of possible variable region contributions to IgG function. The segmental flexibility and complement fixation activity were measured of six genetically engineered molecules (the four human IgG isotypes, mouse IgG3 and rabbit IgG) and the remaining three mouse IgG isotypes, (IgG1, IgG2a and IgG2b), isolated previously by somatic cell genetic techniques. These properties of antibody molecules each correlate with the length of the immunoglobulin hinge region which separate the first and second CH (CH1 and CH2)domains. These results attribute a structural basis for two critical properties of antibody molcules.