## 3 Results and Discussion
### Characterization of Monoclonal Antibodies by the ELISA
\begin{table}
\begin{tabular}{c c c c c c} \hline \hline
**Clone** & \(\mathbf{k_{a}}\), & \(\mathbf{k_{d}}\) & \(\mathbf{K_{A_{s}}}\) & \(\mathbf{K_{D_{s}}}\) & \(\mathbf{\chi^{2}}\) \\  & \(\mathbf{\mathrm{M^{-1}}\times\mathrm{c^{-1}}}\) & \(\mathbf{\mathrm{c^{-1}}}\) & \(\mathbf{\mathrm{M^{-1}}}\) & \(\mathbf{\mathrm{M}}\) & \\ \hline
1B4 & \((2.0\pm 0.5)\times 10^{5}\) & \((7.1\pm 1.6)\times 10^{-5}\) & \((3.6\pm 1.0)\times 10^{9}\) & \((4.7\pm 1.6)\times 10^{-10}\) & 0.104 \\
4E2 cc & \((2.4\pm 0.6)\times 10^{5}\) & \((5.1\pm 1.7)\times 10^{-5}\) & \((7.6\pm 3.2)\times 10^{9}\) & \((2.9\pm 1.1)\times 10^{-10}\) & 0.842 \\
7C3 & \((6.5\pm 3.4)\times 10^{5}\) & \((3.2\pm 0.8)\times 10^{-4}\) & \((2.8\pm 1.0)\times 10^{9}\) & \((1.8\pm 1.3)\times 10^{-9}\) & 0.158 \\ MyoA6 & \((6.3\pm 1.4)\times 10^{4}\) & \((2.8\pm 0.1)\times 10^{-4}\) & \((2.2\pm 0.5)\times 10^{8}\) & \((5.9\pm 1.6)\times 10^{-9}\) & 0.196 \\ MyoB1 & \((5.0\pm 1.2)\times 10^{4}\) & \((3.6\pm 0.5)\times 10^{-3}\) & \((1.4\pm 0.3)\times 10^{7}\) & \((9.6\pm 3.4)\times 10^{-8}\) & 0.227 \\ MyoB12 & \((3.7\pm 0.8)\times 10^{4}\) & \((3.6\pm 0.5)\times 10^{-3}\) & \((7.1\pm 1.6)\times 10^{6}\) & \((1.8\pm 0.3)\times 10^{-7}\) & 0.122 \\ MyoD4 & \((1.2\pm 0.3)\times 10^{5}\) & \((7.0\pm 2.0)\times 10^{-5}\) & \((1.9\pm 0.3)\times 10^{9}\) & \((6.2\pm 1.3)\times 10^{-10}\) & 0.287 \\ MyoE4 & \((1.5\pm 0.2)\times 10^{5}\) & \((5.1\pm 0.8)\times 10^{-4}\) & \((3.4\pm 0.7)\times 10^{8}\) & \((3.9\pm 1.0)\times 10^{-9}\) & 0.124 \\ MyoF5 & \((1.9\pm 0.4)\times 10^{5}\) & \((6.2\pm 2.1)\times 10^{-5}\) & \((6.1\pm 3.7)\times 10^{9}\) & \((4.1\pm 1.8)\times 10^{-10}\) & 0.085 \\ MyoF7 & \((1.4\pm 0.2)\times 10^{5}\) & \((1.2\pm 0.3)\times 10^{-3}\) & \((1.8\pm 0.7)\times 10^{8}\) & \((9.6\pm 3.3)\times 10^{-9}\) & 0.138 \\ MyoH9 & \((8.7\pm 3.1)\times 10^{4}\) & \((4.6\pm 1.5)\times 10^{-4}\) & \((3.2\pm 1.4)\times 10^{8}\) & \((7.3\pm 4.1)\times 10^{-9}\) & 0.265 \\ MyoH11 & \((3.0\pm 0.9)\times 10^{5}\) & \((8.3\pm 0.6)\times 10^{-4}\) & \((3.9\pm 1.5)\times 10^{8}\) & \((4.8\pm 1.2)\times 10^{-9}\) & 0.091 \\ \hline \hline \end{tabular} \(k_{a}\), kinetic association constant; \(k_{d}\), kinetic dissociation constant; \(K_{A}\), equilibrium association constant; \(K_{D}\), equilibrium dissociation constant.  
\end{table} 
Table 1: Analytical parameters of association and dissociation of antibody–myoglobin (MG) complexes. The probable reason for the absence or low intensity of the analytical signal for the remaining combinations is the coincidence or close location of epitopes on the surface of the MG molecule, which prevented the formation of a detectable antibody-antigen-antibody complex on the surface of the carrier. In addition, it should be noted that although antibodies selected for the formation of triple complexes were characterized by relatively high association constants (see Table 1), there was no strong correlation between their affinity and analytical characteristics of the ELISA. Because the experimental conditions (duration of steps and sequence of reagents' addition) were different during measurements of binding constants, the ELISA and LFIA, the combination that provided the maximum sensitivity in the ELISA (7C3/4E2 cc-biotin), was not considered to be a priori optimal for this analysis. Hence, a comparative study was carried out for all eight combinations of antibodies indicated in Table 2. According to the study of [PERSON] et al., the MG content in pork is approximately 2 mg g\({}^{-1}\)[31]. Therefore, the ELISA characteristics of the selected pairs of antibodies indicate their suitability for the development of the LFIA with the, practically, demanded sensitivity.