Selective modification and purification of phosphopeptides for automated sequence analysis

Thomas Soderling, Kenneth Walsh

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

A method is described for the selective purification of 32P-labeled peptides for sequence analysis. The procedure is based on the differential retention on reversed-phase high-performance liquid chromatography of the peptide containing phosphoserine versus dehydroalanine obtained by alkaline β-elimination of the phosphate. The method was tested using two synthetic phosphopeptides representing the phosphorylation site in pyruvate kinase and one of the sites in glycogen synthase.

Original languageEnglish (US)
Pages (from-to)243-251
Number of pages9
JournalJournal of Chromatography A
Volume253
Issue numberC
DOIs
StatePublished - 1982
Externally publishedYes

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Phosphopeptides
Purification
Sequence Analysis
Phosphoserine
Glycogen Synthase
Peptides
Phosphorylation
Pyruvate Kinase
High performance liquid chromatography
Phosphates
Protein Sequence Analysis
Reverse-Phase Chromatography
High Pressure Liquid Chromatography
dehydroalanine

ASJC Scopus subject areas

  • Analytical Chemistry

Cite this

Selective modification and purification of phosphopeptides for automated sequence analysis. / Soderling, Thomas; Walsh, Kenneth.

In: Journal of Chromatography A, Vol. 253, No. C, 1982, p. 243-251.

Research output: Contribution to journalArticle

Soderling, Thomas ; Walsh, Kenneth. / Selective modification and purification of phosphopeptides for automated sequence analysis. In: Journal of Chromatography A. 1982 ; Vol. 253, No. C. pp. 243-251.
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