Dangl J L, Wensel T G, Morrison S L, Stryer L, Herzenberg L A, Oi V T
Department of Genetics, Stanford University, CA 94305.
EMBO J. 1988 Jul;7(7):1989-94. doi: 10.1002/j.1460-2075.1988.tb03037.x.
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 molecules.
我们构建了一组嵌合免疫球蛋白G(IgG)分子,它们对于丹磺酰基(DNS)半抗原具有相同的抗原结合位点,并结合了九个重链恒定(CH)区。这组抗体分子能够比较依赖CH的特性,而不受可变区对IgG功能可能产生的影响。我们测量了六个基因工程分子(四种人IgG亚型、小鼠IgG3和兔IgG)以及先前通过体细胞遗传学技术分离出的其余三种小鼠IgG亚型(IgG1、IgG2a和IgG2b)的片段柔韧性和补体固定活性。抗体分子的这些特性均与分隔第一和第二CH(CH1和CH2)结构域的免疫球蛋白铰链区长度相关。这些结果为抗体分子的两个关键特性奠定了结构基础。