Existence of distinct tyrosylprotein sulfotransferase genes: molecular characterization of tyrosylprotein sulfotransferase-2.

@article{Beisswanger1998ExistenceOD,
  title={Existence of distinct tyrosylprotein sulfotransferase genes: molecular characterization of tyrosylprotein sulfotransferase-2.},
  author={R Beisswanger and Denis Corbeil and C Vannier and Christoph Thiele and Ulrike Dohrmann and Roland Kellner and Keith Ashman and Christof Niehrs and Wieland B Huttner},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1998},
  volume={95 19},
  pages={11134-9}
}
Tyrosylprotein sulfotransferase (TPST) is a 54- to 50-kDa integral membrane glycoprotein of the trans-Golgi network found in essentially all tissues investigated, catalyzing the tyrosine O-sulfation of soluble and membrane proteins passing through this compartment. Here we describe (i) an approach to identify the TPST protein, referred to as MSC (modification after substrate crosslinking) labeling, which is based on the crosslinking of a substrate peptide to TPST followed by intramolecular [35S… CONTINUE READING

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Beisswanger et al

  • Y. Hashimoto, A. Orellana, G. Gil, Hirschberg, C. B. J. Biol. Chem. 267, 15744–15750. FIG. 5. Northern blot analysis showing the distrib Biochemistry
  • Proc. Natl. Acad. Sci. USA 95
  • 1998
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