Szedlacsek S E, Ostafe V, Mogoş S, Hulea S A
Biochem Int. 1986 Feb;12(2):279-89.
A graphical method for the simultaneous determination of the activity of two isoenzymes in a mixture, is presented. The method is based on the different kinetic behaviour of the isoenzymes to the changes in the substrate concentrations. Having determined the reaction rates for the enzyme mixture at different substrate concentrations, the activity of both isoenzymes can be derived graphically. An algebraic method for two or more isoenzymes is mentioned, as well. The applications of the graphical and the algebraic method to A2 and A3 horseradish isoperoxidases demonstrated that the difference between the actual activities of the two isoperoxidases and those determined by the proposed method was around 5% of the actual activities. The scope of application of this method could be extended to isoenzymes of clinical importance.
本文提出了一种同时测定混合物中两种同工酶活性的图解法。该方法基于同工酶对底物浓度变化的不同动力学行为。在确定了酶混合物在不同底物浓度下的反应速率后，两种同工酶的活性均可通过图解法得出。文中还提到了针对两种或更多种同工酶的代数法。图解法和代数法在A2和A3辣根过氧化物酶上的应用表明，两种过氧化物酶的实际活性与用该方法测定的活性之间的差异约为实际活性的5%。该方法的应用范围可扩展到具有临床重要性的同工酶。
