Aasted B, Sogn J A, Kindt T J
J Immunol. 1976 Feb;116(2):387-91.
The L chains of rabbit antibodies directed against group a allotypes exhibited in many instances a high degree of homogeneity as measured by L chain banding patterns in alkaline urea polyacrylamide gels. Amino terminal sequence analyses were carried out on six L chain preparations from antibodies isolated from individual antisera or from pools of antisera. The same major amino terminal sequence, Ala-Val-Val-Met, was observed for each of these preparations indication that anti-allotype antibodies preferentially select L chains from a single subgroup. The antiallotype anitbodies were isolated from antisera by elution from IgG immunoadsorbent columns in yields ranging from 0.3 to 1 mg/ml antibody. The specificity of the isolated antibodies was demonstrated by radioimmune assays. Certain fractions were contaminated with a protein that had properties similar to rabbit serum albumin. This contamination was minimized by preadsorption of the antisera. The antibodies were primarily of the IgG class as shown by immunoelectrophoresis and by m.w. of the H and L chains on SDS gels.
通过碱性尿素聚丙烯酰胺凝胶中的轻链条带模式测量，针对a组同种异型的兔抗体轻链在许多情况下表现出高度的同质性。对从个体抗血清或抗血清池中分离的抗体的六种轻链制剂进行了氨基末端序列分析。对于这些制剂中的每一种，都观察到相同的主要氨基末端序列，即丙氨酸-缬氨酸-缬氨酸-甲硫氨酸，这表明抗同种异型抗体优先从单个亚组中选择轻链。抗同种异型抗体通过从IgG免疫吸附柱上洗脱从抗血清中分离出来，产量范围为0.3至1毫克/毫升抗体。通过放射免疫测定证明了分离抗体的特异性。某些级分被一种性质类似于兔血清白蛋白的蛋白质污染。通过抗血清的预吸附将这种污染降至最低。如免疫电泳和SDS凝胶上重链和轻链的分子量所示，这些抗体主要属于IgG类。
