[Equilibrium and kinetic parameters of the interaction of strophanthin K and its peroxidase conjugates with soluble and immobilized specific antibodies].
Using solid phase enzyme-linked immunoassay (ELISA), rate constants for the formation and dissociation as well as equilibrium dissociation constants for strophanthin complexes interaction with specific antibodies (both soluble and immobilized on activated polystyrene beads and polyamide membranes) have been determined. A satisfactory correlation was found between dissociation constants for immune complexes determined by ELISA (both soluble and immobilized ones) and associations constants for these complexes determined by the Scatchard method. The experimental values of kinetic and equilibrium constants for strophanthin K and its peroxidase complexes interaction reflect the difference in the nature of interacting particles and their environment. Strophanthin complexes with antibodies appeared to be more stable when formed on adsorbents (in comparison with those formed in solution). Strophanthin interaction with immobilized antibodies occurred at a slower rate than that with soluble antibodies. Strophanthin reacts with antibodies more readily than its complexes both in solution and on solid matrices of various polymeric nature.
Tarun
E I
EI
Savenkova
M I
MI
Metelitsa
D I
DI
D001323:Autoantibodies / Q000737:chemistry*; D004797:Enzyme-Linked Immunosorbent Assay; D006735:Horseradish Peroxidase / Q000737:chemistry*; D007700:Kinetics; D012995:Solubility; D013328:Strophanthins / Q000737:chemistry*
D001323:Autoantibodies; D013328:Strophanthins; D006735:Horseradish Peroxidase; C029082:strophanthin K
Ravnovesnye i kineticheskie parametry vzaimodeĭstviia strofantina K i ego pereoksidaznykh kon''iugatov s rastvorennymi i immobilizovannymi spetsificheskimi antitelami.