Characterization of a novel human UDP‐GalNAc transferase, pp‐GalNAc‐T101

FEBS Letters

Togayachi, Akira¹  Hiruma, Toru¹  Kameyama, Akihiko¹  Cheng, Lamei¹  Kudo, Takashi¹  Narimatsu, Hisashi¹  Iwasaki, Hiroko¹  Kahori Tachibana, Kahori¹  Tachibana, Kouichi¹  Guo, Jian-ming¹  Zhang, Yan¹  Wang, Han¹ 

[1]Glycogene 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

关键词: Glycosylation;    Polypeptide N-acetylgalactosaminyltransferase;    O-Glycosylation;    O-Glycan;    Mucin;    pp-GalNAc-T;    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase;    PCR;    polymerase chain reaction;    HPLC;    high-performance liquid chromatography;    FAM;    5-carboxyfluorescein succinimidyl ester;    TFA;    trifluoroacetic acid;    MALDI-TOF;    matrix-assisted laser desorption/ionization time-of-flight;   

DOI  :  10.1016/S0014-5793(02)03399-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown