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Since proteins are separated by nondenaturing electrophoresis in their native form, they generally retain biological activity. In the particular case of enzymes, catalytic activity can be used as a speci c stain for the enzyme in a process called activity staining. This involves use of an arti cial substrate which is converted to an insoluble, coloured product by the catalytic cycle. The location of the protein in the gel can be visualized by observation of the insoluble (and therefore precipitated) product. Since a single enzyme may go through many thousands of catalytic cycles in a few minutes, very tiny amounts of enzyme can be visualized in this way. Although in principle an individual activity stain is required for each enzyme, in practice particular activity stains are available for groups of enzymes sharing a common catalytic process. For example, many dehydrogenases catalyze formation of NADH from NAD. This can be used to reduce tetrazolium to produce insoluble formazan (Figure 5.6). If, after nondenaturing electrophoresis, a gel is soaked with tetrazolium together with appropriate substrates and cofactors for a particular dehydrogenase, formazan will only form where the enzyme is located in the gel. By selecting substrates speci c for the particular dehydrogenase under investigation (e.g. succinate for succinate dehydrogenase, malate for malate dehydrogenase) highly individual staining for dehydrogenases can be achieved using essentially the same staining procedure. This type of experiment is useful in identifying which band among several visible on a nondenaturing gel is the band representing the enzyme of interest. It is also asp.net ean 13 EAN - 13 ASP . NET Control - EAN - 13 barcode generator with free ...
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