Sheets E D, Chen L, Thompson N L
Department of Chemistry, University of North Carolina, Chapel Hill 27599-3290, USA.
Mol Immunol. 1997 May;34(7):519-26. doi: 10.1016/s0161-5890(97)00057-6.
Total internal reflection fluorescence microscopy has been used to examine the interaction of a mouse monoclonal IgG2b, in the absence and presence of its protein antigen, with mouse Fc gamma RII in substrate-supported planar membranes. Equilibrium association and kinetic dissociation constants were measured for the antibody S6-34.11, which is specific for bovine prothrombin fragment 1 (BF1). These measurements showed that BF1 induces a statistically significant decrease (30-40%) in the IgG-Fc gamma RII dissociation kinetics. A corresponding increase in the equilibrium association constant was not observed, perhaps because the statistical accuracy of the equilibrium measurements is lower than that for the kinetic measurements. The consequences of these results for understanding the mechanism by which macrophages recognize and ingest opsonized targets are discussed.
全内反射荧光显微镜已被用于研究一种小鼠单克隆IgG2b在不存在和存在其蛋白质抗原的情况下，与底物支持的平面膜中的小鼠FcγRII的相互作用。测定了针对牛凝血酶原片段1（BF1）的抗体S6-34.11的平衡缔合常数和动力学解离常数。这些测量结果表明，BF1在IgG-FcγRII解离动力学中引起了具有统计学意义的降低（30-40%）。未观察到平衡缔合常数相应增加，这可能是因为平衡测量的统计精度低于动力学测量。讨论了这些结果对于理解巨噬细胞识别和摄取调理素化靶标的机制的影响。
