Distinct orders of GalNAc incorporation into a peptide with consecutive threonines.
Biochem Biophys Res Commun
; 287(1): 110-5, 2001 Sep 14.
Article
em En
| MEDLINE
| ID: mdl-11549261
ABSTRACT
Mucin O-glycosylation is initiated by a transfer of N-acetyl-d-galactosamine (GalNAc) to Ser and Thr residues in polypeptides with a family of UDP-GalNAcpolypeptide N-acetylgalactosaminyltransferases (pp-GalNAc-Ts). In this paper, four human pp-GalNAc-Ts (pp-GalNAc-T1, T2, T3, and T4) were tested for their preferential orders of GalNAc incorporation into FITC-PTTTPITTTTK, a portion of the tandem repeat of human MUC2. The products were separated by reverse-phase HPLC and characterized by MALDI-TOF MS and peptide sequencing. pp-GalNAc-T1 showed preference for acceptor sites, but the order of the incorporation into these sites seemed to be random. In contrast, the GalNAc incorporation by pp-GalNAc-T2, T3, or T4 was not only site-specific but also according to the specific orders. Furthermore, pp-GalNAc-T2, T3, or T4 had distinct maximum numbers of GalNAc incorporations into this peptide.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Acetilgalactosamina
/
Mucinas
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
2001
Tipo de documento:
Article
País de afiliação:
Japão