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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Published in | Journal of chromatography Vol. 397; p. 113 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
26.06.1987
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Subjects | |
Online Access | Get more information |
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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. |
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