Metelitsa D I, Savenkova M I, Kurchenko V P
Prikl Biokhim Mikrobiol. 1987 Jan-Feb;23(1):116-24.
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.
研究了8种芳香胺过氧化的稳态动力学。发现对苯二胺、邻联茴香胺（o-DA）和3,5,3',5'-四甲基联苯胺是辣根过氧化物酶的最佳底物。还研究了用三分子毒毛旋花子苷K修饰的辣根过氧化物酶氧化这些底物的动力学。在37至53摄氏度的温度范围内，测定了过氧化物酶及其与毒毛旋花子苷K的缀合物的失活速率常数。研究了糖和多元醇对过氧化物酶-毒毛旋花子苷K缀合物热稳定性的影响。对o-DA及其与葡聚糖的缀合物的氧化进行了比较动力学研究。所得结果为从植物原料中分离强心苷时进行酶免疫测定奠定了基础。
