Catalase general properties

Figure 6.3 shows catalase transformation under the substrate (ROOH) effect in complex II to be the predominant pathway. For neutral substrates, which are hydroperoxides, the rate of complex II formation is independent of pH and is usually described by the second-order equation [103, 104], Complex II is the general intermediate for catalase and peroxidase reactions with the only difference that for catalase it is colored green (unpaired electron is localized on heme) and for peroxidase it is red (unpaired electron is localized on distal amino-acid fragment). Complex III is also colored red for peroxidase. However, the formation mechanism is different. Complexes II, III and IV are typical of peroxidases, whereas for catalase only complex II is formed. At the stage of complex II formation, the general properties and distinctive features of catalase and peroxidase were determined. 

For the determination of binding properties of biotinylated proteins and conjugates, use flexible 96-wells microplates (Nunc). The general design of the method is similar to classical enzyme-linked immunosorbent assay (ELISA) and RIA methods. Use the described procedure for immobilization of streptavidin, antigen, biotinylated or nonmodified antibody, or catalase. 

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