| Literature DB >> 15147861 |
Lamei Cheng1, Kouichi Tachibana, Hiroko Iwasaki, Akihiko Kameyama, Yan Zhang, Tomomi Kubota, Toru Hiruma, Kahori Tachibana, Takashi Kudo, Jian-Ming Guo, Hisashi Narimatsu.
Abstract
We have cloned, expressed and characterized a novel member of the human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family, pp-GalNAc-T15. The pp-GalNAc-T15 transcript was ubiquitously expressed in human tissues. Recombinant pp-GalNAc-T15 transferred N-acetylgalactosamine (GalNAc) toward a panel of mucin-derived peptide substrates in vitro. Although pp-GalNAc-T15 showed significantly less catalytic activity than pp-GalNAc-T2, T15 transferred up to seven GalNAcs to the Muc5AC peptide, while T2 transferred up to five GalNAcs. These results clearly indicated that pp-GalNAc-T15 is a novel member of the human pp-GalNAc-T family with unique catalytic activity.Entities:
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Year: 2004 PMID： 15147861 DOI： 10.1016/j.febslet.2004.03.108
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124