Blank U, Daëron M, Galinha A, Malard V, Fridman W H, Sautès C
INSERM U.255, Institut Curie, Paris, France.
Mol Immunol. 1989 Feb;26(2):107-14. doi: 10.1016/0161-5890(89)90091-6.
Suppressor murine IgG-BF produced by the T cell hybrid (T2D4) expressing low affinity Fc gamma R (Fc gamma RII) contain four biologically active polypeptides of pI 5.2, 6.3, 7.7 and 8.3, respectively. They were fractionated by affinity chromatography on immunoadsorbents coupled with F(ab')2 fragments of the monoclonal anti-Fc gamma RII antibody 2.4G2 and by hydrophobic interaction chromatography. Both methods led to the identification of biologically active IgG-BF which react with 2.4G2 and of IgG-BF which do not react with 2.4G2. Molecules bearing the epitope recognized by 2.4G2 had an apparent pI of 5.3 while the pI of those which did not express this epitope were 6.3, 7.8 and 8.5, respectively. Therefore, one IgG-BF polypeptide of pI 5.3 is probably related to Fc gamma RII.
由表达低亲和力FcγR(FcγRII)的T细胞杂交体(T2D4)产生的抑制性小鼠IgG-BF包含四种分别具有5.2、6.3、7.7和8.3等生物学活性的多肽。它们通过在与单克隆抗FcγRII抗体2.4G2的F(ab')2片段偶联的免疫吸附剂上进行亲和层析以及通过疏水相互作用层析进行分离。两种方法都鉴定出了与2.4G2反应的具有生物学活性的IgG-BF以及不与2.4G2反应的IgG-BF。带有2.4G2识别表位的分子表观pI为5.3,而那些不表达该表位的分子的pI分别为6.3、7.8和8.5。因此,一种pI为5.3的IgG-BF多肽可能与FcγRII相关。