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- W1509211541 abstract "Identification of O-phosphorylated amino acids within the primary structure of regulatory proteins is important in understanding the mechanisms by which their functions are regulated. In many cases radioactive labeling with [32P]phosphate is tedious or sometimes impossible. Therefore, we have established a series of new non-radioactive methods that permit the localization of phosphoserine, phosphothreonine, and phosphotyrosine. After partial hydrolysis of a phosphopeptide or phosphoprotein, phosphoserine, phosphothreonine, or phosphotyrosine are determined by capillary electrophoresis as their dabsyl-derivatives. Chemical modification transforms phosphoserine or phosphothreonine to S-ethylcysteine or β-methyl-S-ethyl-cysteine, respectively, allowing their localization during sequence analysis. We apply solid-phase sequencing to overcome the limitations of the gas-phase sequenator in the case of phosphotyrosinecontaining peptides. Liquid chromatography on-line connected to an electrospray mass spectrometer is a powerful new method of increasing importance in the protein chemistry field. It is especially well suited for identification of phosphoserine- or phosphothreonine-containing peptides in a proteolytic digest of a phosphoprotein. In this article we will describe how to work with these new methods practically.—Meyer, H. E., Eisermann, B., Heber, M., Hoffmann-Posorske, E., Korte, H., Weigt, C., Wegner, A., Hutton, T., Donella-Deana, A., Perich, J. W. Strategies for nonradioactive methods in the localization of phosphorylated amino acids in proteins. FASEB J. 7: 776-782; 1993." @default.
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- W1509211541 date "1993-06-01" @default.
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- W1509211541 title "Strategies for nonradioactive methods in the localization of phosphorylated amino acids in proteins <sup>1</sup>" @default.
- W1509211541 doi "https://doi.org/10.1096/fasebj.7.9.7687226" @default.
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