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FEBS Lett. 2002 Nov 6;531(2):115-21.

Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T10.

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  • 1Glycogene Function Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), Central-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan.


A novel member of the human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) gene family was cloned as a homolog of human pp-GalNAc-T7, and designated pp-GalNAc-T10. pp-GalNAc-T10 transcript was found in the small intestine, stomach, pancreas, ovary, thyroid gland and spleen. In a polypeptide GalNAc-transfer assay, recombinant pp-GalNAc-T10 transferred GalNAc onto a panel of mucin-derived peptide substrates. Furthermore, pp-GalNAc-T10 demonstrated strong transferase activity with glycopeptide substrates.

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