Find catalase in the plants by using bradford regent, but why use only bradford regent in to catalase assay, i asked this, because of that supernatant contains other oxidase enzymes and proteins . If the connection have in between bradford regent and uv spectrophotometer absorbance, What is that?why use 240nm for catalase assay?
I am not sure I understood your question, but here is some information:
1. A common method to measure catalase activity is to monitor the decomposition of hydrogen peroxide at 240 nm using the molar absorptivity of H2O2 at 240 nm of 0.0394 mM-1 cm-1. This was originally described by Aebi in 1984. See: Article [13] Catalase in vitro
2. The Bradford assay, on the other hand, is widely used to estimate the concentration of soluble protein in a sample. See: Article A Rapid and Sensitive Method for Quantitation of Microgram Q...
3. The concentration of soluble proteins in homogenates/extracts is often used to normalize the activity of enzymes, resulting in expressing enzymatic activity in terms of U per mg of protein. For example, see: Article Roles of catalase and glutathione peroxidase in the toleranc...
4. There are several other methods to measure catalase activity, but the Bradford assay is not one of them.
The principle of this assay is that the binding of protein molecules to Coomassie dye under acidic conditions results in a color change from brown to blue.
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