Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3.

@article{Wandall1997SubstrateSO,
  title={Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3.},
  author={Hans H. Wandall and Helle Hassan and Ekaterina Mirgorodskaya and Anne K. Kristensen and Peter Roepstorff and Eric P. Bennett and Peter Aagaard Nielsen and Michael Anthony Hollingsworth and Joy Burchell and Joyce Taylor-Papadimitriou and Henrik Clausen},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 38},
  pages={23503-14}
}
Mucin-type O-glycosylation is initiated by UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferases). The role each GalNAc-transferase plays in O-glycosylation is unclear. In this report we characterized the specificity and kinetic properties of three purified recombinant GalNAc-transferases. GalNAc-T1, -T2, and -T3 were… CONTINUE READING