Singh V
Indian J Exp Biol. 1989 Jan;27(1):5-9.
Monoclonal anti-GnRH antibodies reacting to the heptapeptide 4-10 (H-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-OH) were isolated by affinity chromatography using Sepharose 4B-heptapeptide (4-10) column. The ELISA additivity test and antibody-antibody competition techniques were used to study whether the affinity purified MoAb (A-MoAb) fraction recognize the sequence or the conformation of the native hormone. All four A-MoAbs, P862, P778, P764 and P813, were able to recognize the common epitope and did not allow to bind the conventional anti-GnRH antibodies (CoAbs) indicating that the CoAbs were conformation specific. Similarly in antibody-antibody competition technique, all A-MoAbs were able to compete with CoAbs, indicating that MoAbs were generated against the conformation of GnRH involving the entire molecule.
使用琼脂糖4B-七肽（4-10）柱通过亲和色谱法分离出与七肽4-10（H-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-OH）反应的单克隆抗促性腺激素释放激素（GnRH）抗体。采用酶联免疫吸附测定（ELISA）加和性试验和抗体-抗体竞争技术，研究亲和纯化的单克隆抗体（A-MoAb）组分是否识别天然激素的序列或构象。所有四种A-MoAb，即P862、P778、P764和P813，都能够识别共同表位，并且不允许传统抗GnRH抗体（CoAbs）结合，这表明CoAbs具有构象特异性。同样，在抗体-抗体竞争技术中，所有A-MoAb都能够与CoAbs竞争，表明所产生的单克隆抗体针对涉及整个分子的GnRH构象。
