EDELMAN G M, HEREMANS J F, HEREMANS M T, KUNKEL H G
J Exp Med. 1960 Jul 1;112(1):203-23. doi: 10.1084/jem.112.1.203.
Two major antigenic fragments were obtained from various purified gamma-globulin preparations after papain treatment. One, the F component, had a mobility faster than the original gamma-globulin and the second, the S component, had a slower mobility. Similar F and S components were also obtained with certain homogeneous myeloma proteins which were closely related to gamma-globulin immunologically. Additional minor antigenic components were detected with certain antisera. The technique of immunoelectrophoresis was particularly useful for bringing out the different antigenic constituents obtained after papain treatment. The F and S components as well as a midfraction were isolated by chromatography on DEAE-cellulose. These were immunologically homogeneous and could be utilized to absorb F and S antibodies from various antisera. The relative amount of F and S antibodies varied in different antisera from individual rabbits immunized with whole gamma-globulin. Whole gamma-globulin was separated by zone electrophoresis into a fast migrating and a more slowly migrating fraction. Each of these gave rise to F and S components after splitting with papain. The F components of the two gamma-globulins were similar in mobility, while the S components showed marked mobility differences although antigenically they were very similar. The mobility differences of the parent gamma-globulin appeared to be primarily related to the differences in the S component. Certain antisera against pathological gamma-globulins were found to give double lines with a wide variety of gamma-globulin preparations in agar diffusion. These were shown to be related to the F and S antigenic determinants of gamma-glubulin. This relationship was evident by a number of procedures utilizing both Ouchterlony plate techniques and immunoelectrophoresis. The question of whether these findings indicate heterogeneity of gamma-globulin in relation to the F and S antigenic components, or whether different antigenic groups on one molecule can give rise to separate lines in certain instances, is discussed.
经木瓜蛋白酶处理后，从各种纯化的γ-球蛋白制剂中获得了两个主要的抗原片段。一个是F组分，其迁移率比原来的γ-球蛋白快，另一个是S组分，迁移率较慢。用某些与γ-球蛋白在免疫学上密切相关的均质骨髓瘤蛋白也获得了类似的F和S组分。用某些抗血清检测到了其他次要的抗原成分。免疫电泳技术对于揭示木瓜蛋白酶处理后获得的不同抗原成分特别有用。通过在DEAE-纤维素上进行色谱分离，分离出了F和S组分以及一个中间级分。这些在免疫学上是均质的，可用于从各种抗血清中吸收F和S抗体。在用全γ-球蛋白免疫的个体兔的不同抗血清中，F和S抗体的相对量有所不同。全γ-球蛋白通过区带电泳被分离成一个快速迁移的级分和一个迁移较慢的级分。用木瓜蛋白酶裂解后，每一个级分都产生了F和S组分。两种γ-球蛋白的F组分迁移率相似，而S组分虽然在抗原性上非常相似，但迁移率有明显差异。母体γ-球蛋白的迁移率差异似乎主要与S组分的差异有关。发现在琼脂扩散中，某些针对病理性γ-球蛋白的抗血清与多种γ-球蛋白制剂产生双线。这些被证明与γ-球蛋白的F和S抗原决定簇有关。通过使用奥克特洛尼平板技术和免疫电泳的一些方法，这种关系很明显。讨论了这些发现是表明γ-球蛋白在F和S抗原成分方面存在异质性，还是表明一个分子上的不同抗原基团在某些情况下可以产生分开的条带这一问题。
