Abstract
A novel member of the human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase gene family, designated GalNAc-T7, was cloned and expressed. GalNAc-T7 exhibited different properties compared to other characterized members of this gene family, in showing apparent exclusive specificity for partially GalNAc-glycosylated acceptor substrates. GalNAc-T7 showed no activity with a large panel of non-glycosylated peptides, but was selectively activated by partial GalNAc glycosylation of peptide substrates derived from the tandem repeats of human MUC2 and rat submaxillary gland mucin. The function of GalNAc-T7 is suggested to be as a follow-up enzyme in the initiation step of O-glycosylation. Copyright (C) 1999 Federation of European Biochemical Societies.
Originalsprog | Engelsk |
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Tidsskrift | FEBS Letters |
Vol/bind | 460 |
Udgave nummer | 2 |
Sider (fra-til) | 226-230 |
Antal sider | 5 |
ISSN | 0014-5793 |
DOI | |
Status | Udgivet - 29 okt. 1999 |