FIG. 5.

F-RhoA interaction analysis by real-time BIA using the BIAcore 2000 instrument. Immunoaffinity-purified F ligand was captured by immobilized anti-F1 monoclonal antibody on the surface of the carboxymethylated dextran sensor chip. An analyte, RhoA, was allowed to flow on the surface of F ligand, and the interaction was recorded on the sensorgram as RU. The RU at baseline (phase a to b) corresponds to the amount of capture ligand immobilized on the sensor chip. Phase b to c corresponds to the injection of analyte. Phase c to d corresponds to the injection of buffer to wash nonspecifically bound analyte molecules. 976RU corresponds to binding of approximately 0.97 ng of RhoA to F per mm² on the sensor chip surface (A). RSV G (B) and Rac1 (C) proteins were used as negative ligand and analyte controls, respectively. The dashed line has been added to more easily show the deflection above baseline when RhoA interacts with F.