Fig 1.
Sensorgram showing the association and dissociation processes of biomolecular interaction between HBsAg and HbsAb.
The data marked with a triangle is obtained in the average of more than three sets of measurement results in RU. This sensorgram is showing that the HBsAg was binding on the specific HBsAb (association phase) starting from the injection point a and reaches an equilibrium after approximately 251s. From the dissociation starting point b, the dissociation phase was formed sequentially. The microfludic cell of this SPR bioanalyzer was kept at a constant temperature of 37°C.
Fig 2.
The fitting results obtained from both Newton Iteration algorithm and Marquardt algorithm.
The data marked with a triangle is obtained in the average of more than three sets of measurement results in RU, and the fitted curve was marked with a solid line. A. The curve-fitting using the Newton Iteration algorithm with the initial value of 0.0095, B. The curve-fitting using the Newton Iteration algorithm with the initial value of 0.011, C. The curve-fitting using the Marquardt algorithm with the initial value of 0.0095, D. The curve-fitting using the Marquardt algorithm with the initial value of 0.011.
Table 1.
Kinetic constants of molecular interaction between HBsAg and HBsAb.