Activity of partially purified UDP-N-acetyl-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase with different peptide acceptors

• Autorzy: Porowska H. , Paszkiewicz-Gadek A. , Gindzienski A.
• Języki publikacji: EN

Abstrakty

EN

As part of investigations on the role of the UDP-GalNAc-ribosome complex in the initial O-glycosylation of proteins, we have isolated from porcine gastric mucosa GalNAc-transferase, mucin and apomucin, and its three fractions containing carbohydrate in the amounts: I - 1.6%, II - 0.65% and III - 0.00% (wt/wt) of apomucin mass. Amino acid analysis showed that fractions I and II contained slightly higher amounts of serine and threonine as compared to native mucin and apomucin. The short peptide Pro-Thr-Ser-Ser-Pro-Ile-Ser-Thr was the most effectively glycosylated. Our apomucin preparations are also good acceptors of GalNAc and can be used for testing of O-glycosylation in vitro.

Słowa kluczowe

EN

peptide acceptor; glycosylation; N-acetylgalactosaminyltransferase; polypeptide; apomucin

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1999
• Tom: 46
• Numer: 2
• Opis fizyczny: p.365-370,fig.

Twórcy

autor

Porowska H.

• Medical Academy, A.Mickiewicza 2a, 15-222 Bialystok, Poland, e-mail: [e-mail]

autor

Paszkiewicz-Gadek A.

autor

Gindzienski A.

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