Ferguson T A, Iverson G M
J Immunol. 1986 Apr 15;136(8):2896-903.
We have used a rat monoclonal antibody (mAb) (called 14-30) to affinity purify the antigen-binding chain of a suppressor inducer factor (TsiF-AB) from the serum of mice hyperimmune to heterologous erythrocytes. The TsiF-AB requires the addition of a second, antigen-nonspecific component for biologic activity as well as Lyt-2+ T cells in the assay culture. This mAb can be used to affinity purify suppressor inducer factor from a well-characterized TsiF but not suppressor effector factor (TseF) from culture supernatants. Binding of mAb 14-30 to TsiF is independent of the antigen specificity of the suppressor factor and of the strain of origin of the TsiF. The TsiF affinity purified from hyperimmune serum has an apparent m.w. of 68,000 by SDS-PAGE analysis. 2D gel analysis shows that the serum-derived TsiF has charge heterogeneity, all in the acid range.
我们使用了一种大鼠单克隆抗体（mAb）（称为14 - 30），从对异源红细胞高度免疫的小鼠血清中亲和纯化抑制诱导因子（TsiF - AB）的抗原结合链。TsiF - AB在分析培养中需要添加第二种非抗原特异性成分以及Lyt - 2⁺ T细胞才能发挥生物学活性。这种单克隆抗体可用于从特征明确的TsiF中亲和纯化抑制诱导因子，但不能从培养上清液中纯化抑制效应因子（TseF）。单克隆抗体14 - 30与TsiF的结合独立于抑制因子的抗原特异性以及TsiF来源的品系。通过SDS - PAGE分析，从高度免疫血清中亲和纯化的TsiF的表观分子量为68,000。二维凝胶分析表明，血清来源的TsiF具有电荷异质性，均在酸性范围内。
