Woof J M, Partridge L J, Jefferis R, Burton D R
Mol Immunol. 1986 Mar;23(3):319-30. doi: 10.1016/0161-5890(86)90059-3.
Earlier studies, which provided indirect evidence for the involvement of the C gamma 2 domain of human immunoglobulin G (IgG) in human immunoglobulin G (IgG) in human monocyte binding, have been extended to further localise the site of interaction on human IgG. A number of IgGs from several different species and fragments of human IgGs were assayed for ability to inhibit the interaction of radio-labelled human IgG and the human monocyte. By comparison of the amino-acid sequences of those IgGs found to exhibit relatively tight, intermediate or weak binding to human monocyte Fc receptors we are able to postulate a possible monocyte-binding site on human IgG. In addition, the results have implications for the applicability of monoclonal antibodies and antisera when used in the presence of human monocytes and possibly macrophages.
早期的研究为人类免疫球蛋白G(IgG)的Cγ2结构域参与人类单核细胞结合提供了间接证据,这些研究已得到扩展,以进一步确定人类IgG上的相互作用位点。对来自几种不同物种的多种IgG以及人类IgG的片段进行了检测,以评估它们抑制放射性标记的人类IgG与人类单核细胞相互作用的能力。通过比较那些被发现与人类单核细胞Fc受体表现出相对紧密、中等或弱结合的IgG的氨基酸序列,我们能够推测出人类IgG上一个可能的单核细胞结合位点。此外,这些结果对于单克隆抗体和抗血清在人类单核细胞以及可能的巨噬细胞存在时的适用性具有重要意义。