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Localization of Endogenous Phosphoserine Residues in the Primary Structure of Proteins

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Methods in Protein Sequence Analysis

Abstract

Localization of phosphorylated amino acids within the primary structure of phosphorylated proteins is a prerequisite for understanding their function. Of particular interest are those residues which are phosphorylated in vivo (endogenous phosphate), since these phospho-amino acids are physiologically relevant e.g. in the regulation of enzyme activities, ion channel mechanisms and other regulatory mechanisms.

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References

  • Dedner N, Meyer HE, Ashton C and Wildner GF (1988) The N-terminal sequence analysis of the 8 kDa protein in Chlamydomonas reinhardii. Localization of the phosphothreonine. FEBS Lett, in press

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  • Meyer HE, Hoffmann-Posorske E, Korte H and Heilmeyer LMG (1986) Sequence analysis of phosphoserine-containing peptides. Modification for picomolar sensitivity. FEBS Lett 204: 61–66

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  • Meyer HE, Hoffmann-Posorske E, Kuhn CC and Heilmeyer LMG (1988) microcharacterization of phosphoserine containing proteins. Localization of the autophosphorylation sites of skeletal muscle phosphorylase kinase. In: Tschesche H (ed) Modern Methods in Protein Chemistry, Vol.3 Walter de Gruyter & Co., Berlin New York, p 185–212

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  • Swiderek K, Jaquet K, Meyer HE and Heilmeyer LMG (1988) Cardiac troponin I, isolated from bovine heart, contains two adjacent phosphoserines. A first example of phosphoserine determination by derivatisation to S-ethylcysteine. Eur J Biochem, in press

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© 1989 Springer-Verlag Berlin Heidelberg

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Meyer, H.E. et al. (1989). Localization of Endogenous Phosphoserine Residues in the Primary Structure of Proteins. In: Wittmann-Liebold, B. (eds) Methods in Protein Sequence Analysis. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-73834-0_4

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  • DOI: https://doi.org/10.1007/978-3-642-73834-0_4

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-73836-4

  • Online ISBN: 978-3-642-73834-0

  • eBook Packages: Springer Book Archive

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