Quantitative determination of phosphoserine by high-performance liquid chromatography as the phenylthiocarbamyl-S-ethylcysteine. Application to picomolar amounts of peptides and proteins

A method is described that permits the phosphoserine content of proteins and peptides to be determined in picomolar amounts. A micro-batch reaction first converts phosphoserine into S-ethylcysteine. Hydrolysis with 6 M hydrochloric acid then yields the free amino acid, which is coupled with phenyl i...

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Bibliographic Details
Published inJournal of chromatography Vol. 397; p. 113
Main Authors Meyer, H E, Swiderek, K, Hoffmann-Posorske, E, Korte, H, Heilmeyer, Jr, L M
Format Journal Article
LanguageEnglish
Published Netherlands 26.06.1987
Subjects
Amino Acids - analysis
Animals
Cattle
Chromatography, High Pressure Liquid
Cysteine - analogs & derivatives
Indicators and Reagents
Oligopeptides - analysis
Peptides - analysis
Phosphorylation
Phosphoserine - analysis
Proteins - analysis
Serine - analogs & derivatives
Troponin - analysis
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Summary:A method is described that permits the phosphoserine content of proteins and peptides to be determined in picomolar amounts. A micro-batch reaction first converts phosphoserine into S-ethylcysteine. Hydrolysis with 6 M hydrochloric acid then yields the free amino acid, which is coupled with phenyl isothiocyanate to give the corresponding phenylthiocarbamylamino acid. This derivative is determined quantitatively in the range 10-20 pmol by reversed-phase high-performance liquid chromatography. The method works well with either small peptides or proteins in the low picomole range.