Abstract
Two-dimensional gel electrophoresis is a well-known technique to detect proteins and identify them by mass spectrometry. Peroxidase activity is commonly revealed in different fields of investigation by adding a substrate to the enzyme in the sample, in the presence of hydrogen peroxide. From these two points, a useful procedure to detect this enzymatic activity on two-dimensional gels is described. The novelty and interest of this technique is that the electrophoresis developed combines a nondenaturing gel with running denaturing conditions, allowing peroxidase activity to remain after the whole process. Therefore, the isoelectric point and the molecular weight can be used to separate different isoforms of peroxidase on a two-dimensional gel.
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