[Optimization of the use of horseradish peroxidase and its antibodies in immunoenzyme analysis].
The steady-state kinetics of peroxidation of 8 aromatic amines was studied. p-Phenylenediamine, o-dianisidine (o-DA) and 3,5,3',5'-tetramethylbenzidine were found to be optimal substrates of horse-radish peroxidase. The kinetics of oxidation of these substrates by horseradish peroxidase modified with three molecules of Strophanthin K was studied as well. Within the temperature range from 37 to 53 degrees C the inactivation rate constants were determined for peroxidase and its conjugate with Strophanthin K. The effect of sugars and polyols on thermal stability of the conjugate peroxidase-Strophanthin K was investigated. A comparative kinetic study was performed of oxidation of o-DA and its conjugate with dextran. The results obtained made a basis for an enzyme immunoassay of cardiac glycosides during their isolation from plant raw material.
D002301:Cardiac Glycosides / Q000032:analysis*; D006735:Horseradish Peroxidase / Q000276:immunology; D007124:Immunoenzyme Techniques; D007700:Kinetics; D010084:Oxidation-Reduction; D010544:Peroxidases; D013328:Strophanthins / Q000032:analysis; D013379:Substrate Specificity
D002301:Cardiac Glycosides; D013328:Strophanthins; D006735:Horseradish Peroxidase; D010544:Peroxidases; C029082:strophanthin K
Optimizatsiia ispol'zovaniia peroksidazy khrena i ee antitel v immunofermentnom analize.