Related Experiment Video
Updated: Jul 6, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Published on: June 21, 2021
Analysis of tyrosine-O-sulfation
Jens R Bundgaard1, Jette W Sen, Anders H Johnsen
1Department of Clinical Biochemistry, Copenhagen University Hospital, Copenhagen, Denmark.
Abstract:
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.
Related Concept Videos
Phase II Reactions: Sulfation and Conjugation with α-Amino Acids
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Proteoglycans
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Protein Glycosylation
Glycosylation occurs in...
Sulfur Assimilation

