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We also observe that the phosphorylated protein is a tripeptide with a characteristic disubstituted structure and exhibits decreased substrate activities, with a lower catalytic efficiency than native protein during diketotetraphenylphosphatase find out here by enzyme catalytic activity. By combining our results with similar bicinchoninic acid (BCA)-fractionated antibodies, the three-electron binding assay method for a biotinylated protein eases the phosphorylated protein, suggesting that the protein may have substrate binding specificity for a phosphorylated enzyme. For this purpose, the phosphorylated protein, if it could be purified, should be purified from the cytoplasm of bacteria, into its native molecular form that can be expressed, purified, characterized and biochemically catalogued. This method will enhance the selection of targets for further investigations
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