Springer Protocols: Abstract: Analysis of Tyrosine-O-Sulfation

Analysis of Tyrosine-O-Sulfation

By: Jens R. Bundgaard³, Jette W. Sen³, Anders H. Johnsen³, Jens F. Rehfeld³

Abstract

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Tyrosine O-sulfation was first described about 50 years ago as a post-translational modification of fibrinogen. In the following 30 years it was considered to be a rare modification affecting only a few proteins and peptides. However, in the beginning of the 1980s tyrosine (Tyr) sulfation was shown to be a common modification and since then an increasing number of proteins have been identified as sulfated. The target proteins belong to the classes of secretory, plasma membrane, and lysosomal proteins, which reflects the intracellular localization of the enzymes catalyzing Tyr sulfation, the tyrosylprotein sulfotransferases (TPSTs).

Traditionally, Tyr sulfation has been analyzed by incorporation of radiolabeled sulfate into target cells followed by purification of the target protein. Subsequently, the protein is degraded enzymatically or by alkaline hydrolysis followed by thin-layer electrophoresis to demonstrate the presence of radioactively labeled tyrosine. These techniques have been described in detail previously. The aim of this chapter is to present alternative analytical methods of Tyr sulfation than radioisotope incorporation before analysis.

Affiliation(s): (3) Department of Clinical Biochemistry, Copenhagen University Hospital, Copenhagen, Denmark

Book Title: Post-translational Modifi cations of Proteins: Tools for Functional Proteomics

Series: Methods in Molecular Biology | Volume: 446 | Pub. Date: Apr-04-2008 | Page Range: 47-66 | DOI: 10.1007/978-1-60327-084-7_4

Subject: Protein Science

Key Words: Tyrosine O-sulfation - tyrosylprotein sulfotransferases - radio-immunoassay - MALDI-TOF

References

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