Identification of tyrosine O-sulfate in proteins by reverse-phase high-performance liquid chromatography: Use of base hydrolysis combined with precolumn derivatization using phenyl isothiocyanate
✍ Scribed by David L. Christie; Rena M. Hill; Kristine Isakow; Peter M. Barling
- Publisher
- Elsevier Science
- Year
- 1986
- Tongue
- English
- Weight
- 637 KB
- Volume
- 154
- Category
- Article
- ISSN
- 0003-2697
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✦ Synopsis
A procedure has been developed for the analysis of tyrosine U-sulfate in proteins. Samples are subjected to base hydrolysis with Ba(OHh. neutralized with sulfuric acid, and the majority of other amino acids removed by chromatography on Dowex AG 50 X 8. The average recovery of tyrosine O-sulfate from these procedures was 43%. Tyrosine O-sulfate was identified by reversephase HPLC as the phenylthiocarbamyl derivative following precolumn derivatization with phenyl isothiocyanate. The method has been applied to bovine fibrinogen giving a tyrosine O-sulfate content ranging from 0.59 to 1.23 mol/mol. These procedures were also shown to be suitable for the analysis of the incorporation of ["S]sulfate into tyrosine O-sulfate residues in proteins by intact Cek.
(a 1986 Academic PES. IIIC.