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

H Porowska; A Paszkiewicz-Gadek; A Gindzieński

doi:10.18388/abp.1999_4169

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

H Porowska Department of General and Organic Chemistry, Medical Academy, Bialystok, Poland.;
A Paszkiewicz-Gadek
A Gindzieński

DOI: https://doi.org/10.18388/abp.1999_4169

Abstract

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.

Published

1999-06-30

Issue

Vol. 46 No. 2 (1999)

Section

Articles

Acta Biochimica Polonica is an OpenAccess quarterly and publishes four issues a year. All contents are distributed under the Creative Commons Attribution-ShareAlike 4.0 International (CC BY 4.0) license. Everybody may use the content following terms: Attribution — You must give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use.