Boyle M D, Wallner W A, von Mering G O, Reis K J, Lawman M J
Mol Immunol. 1985 Sep;22(9):1115-21. doi: 10.1016/0161-5890(85)90115-4.
The interaction of type I (staphylococcal protein A) and type III (streptococcal FcRc) bacterial Fc receptors with goat immunoglobulins has been studied. Staphylococcal protein A bound poorly to the majority of goat immunoglobulins at all pHs tested. There was some evidence that protein A bound IgG2 better than IgG1, particularly at pH 8 and above. One of 10 sera tested demonstrated a high level of reactivity with protein A and this was shown to correlate with the presence of a natural antibody to protein A. The streptococcal Fc receptors, FcRc, bound efficiently to all goat IgG and goat sera tested. Both goat IgG subclasses reacted efficiently with the FcRc between pH 6 and 8. Inhibition of binding of 125I-FcRc to immobilized goat IgG enabled levels of IgG in goat serum to be estimated. These results suggest the streptococcal FcRc will be of value as an immunochemical reagent in studies involving isolation and quantitation of goat immunoglobulins.
对I型(葡萄球菌蛋白A)和III型(链球菌FcRc)细菌Fc受体与山羊免疫球蛋白的相互作用进行了研究。在所有测试的pH值下,葡萄球菌蛋白A与大多数山羊免疫球蛋白的结合都很差。有证据表明,蛋白A与IgG2的结合优于IgG1,尤其是在pH 8及以上时。所测试的10份血清中有一份显示出与蛋白A的高反应性,并且这被证明与存在针对蛋白A的天然抗体相关。链球菌Fc受体FcRc与所有测试的山羊IgG和山羊血清有效结合。两种山羊IgG亚类在pH 6至8之间均与FcRc有效反应。125I-FcRc与固定化山羊IgG结合的抑制作用使得能够估计山羊血清中IgG的水平。这些结果表明,链球菌FcRc作为一种免疫化学试剂,在涉及山羊免疫球蛋白分离和定量的研究中将具有价值。