cDNA cloning and expression of a novel human UDP-N-acetyl-α-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3
EP Bennett, H Hassan, H Clausen - Journal of Biological Chemistry, 1996 - ASBMB
The glycosylation of serine and threonine residues during mucin-type O-linked protein
glycosylation is carried out by a family of UDP-GalNAc: polypeptide N-
acetylgalactosaminyltransferases (GalNAc-transferase). Previously two members, GalNAc-
T1 and− T2, have been isolated and the genes cloned and characterized. Here we report
the cDNA cloning and expression of a novel GalNAc-transferase termed GalNAc-T3. The
gene was isolated and cloned based on the identification of a GalNAc-transferase motif (61 …
glycosylation is carried out by a family of UDP-GalNAc: polypeptide N-
acetylgalactosaminyltransferases (GalNAc-transferase). Previously two members, GalNAc-
T1 and− T2, have been isolated and the genes cloned and characterized. Here we report
the cDNA cloning and expression of a novel GalNAc-transferase termed GalNAc-T3. The
gene was isolated and cloned based on the identification of a GalNAc-transferase motif (61 …
