Sulfation was first discovered by Bettelheim in bovine fibrinopeptide B in 1954[1] and later found to be present in animals and plants but not in prokaryotes or in yeast.
Sulfation sites are tyrosine residues exposed on the surface of the protein typically surrounded by acidic residues; a detailed description of the characteristics of the sulfation site was available from PROSITE[3] and predicted by an on-line tool named the Sulfinator.
There is very limited evidence that the TPST genes are subject to transcriptional regulation and tyrosine O-sulfate is very stable and cannot be easily degraded by mammalian sulfatases.
[8] In 2006, an article was published in the Journal of Biological Chemistry describing the production and characterization of an antibody called PSG2.
This antibody shows exquisite sensitivity and specificity for epitopes containing sulfotyrosine independent of the sequence context.