Ramasamy R, Richardson N E, Feinstein A
Immunology. 1976 Jun;30(6):851-8.
It is shown that the Fc receptor for IgG on lymph node cells recognizes IgG molecules of mouse IgG1, IgG2a and IgG2b subclasses. The presence of an intact CH3 domain is required to bind IgG to the Fc receptors. While monomeric IgG molecules are shown to bind to Fc receptors, heat aggregated IgG was found to bind more efficiently. The various forms of IgM molecules investigated show only weak or no binding in comparison. The significance of these results is discussed with relevance to the possible biological function of the Fc receptors on lymphocytes.
研究表明,淋巴结细胞上的IgG Fc受体可识别小鼠IgG1、IgG2a和IgG2b亚类的IgG分子。完整的CH3结构域的存在是IgG与Fc受体结合所必需的。虽然单体IgG分子可与Fc受体结合,但发现热聚集的IgG结合效率更高。相比之下,所研究的各种形式的IgM分子仅表现出微弱的结合或不结合。结合淋巴细胞上Fc受体可能的生物学功能对这些结果的意义进行了讨论。