Mahana W, Jacquemart F, Ermonval M
Unité d'Immunocytochimie, Institut Pasteur, Paris, France.
Scand J Immunol. 1994 Jan;39(1):107-10. doi: 10.1111/j.1365-3083.1994.tb03347.x.
N12.12 is a monoclonal immunoglobulin (Ig) kappa light chain (KLC) secreted by a B-cell hybridoma derived from spleen cells of a normal SJA mouse. No heavy chain was detected in the culture supernatant of this hybridoma using an enzyme immunoassay (EIA) and after polyacrylamide gel electrophoresis (SDS-PAGE) of the 35S-methionin biosynthetically labelled proteins secreted by the cells. It was shown that N12.12 KLC reacted with mouse actin, trinitrophenylated bovine serum albumin (TNP25-BSA) and weakly with bovine myoglobin. The binding of the N12.12 'monoclonal antibody' to mouse actin or to TNP25-BSA was inhibited specifically by both antigens with a dissociation constant (KD) for binding to mouse actin of 10(-7) M. The results indicate that a free KLC can bind both to mouse and to non-mouse molecules, thus exhibiting binding characteristics usually attributed to natural multireactive antibodies.
N12.12是一种单克隆免疫球蛋白（Ig）κ轻链（KLC），由源自正常SJA小鼠脾细胞的B细胞杂交瘤分泌。使用酶免疫测定（EIA）以及对细胞分泌的经35S-蛋氨酸生物合成标记的蛋白质进行聚丙烯酰胺凝胶电泳（SDS-PAGE）后，在该杂交瘤的培养上清液中未检测到重链。结果表明，N12.12 KLC与小鼠肌动蛋白、三硝基苯基化牛血清白蛋白（TNP25-BSA）反应，与牛肌红蛋白反应较弱。N12.12“单克隆抗体”与小鼠肌动蛋白或TNP25-BSA的结合被两种抗原特异性抑制，与小鼠肌动蛋白结合的解离常数（KD）为10^(-7) M。结果表明，游离的KLC可以与小鼠和非小鼠分子结合，从而表现出通常归因于天然多反应性抗体的结合特性。
