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PMID: 3944078 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Asparaginyl-N-acetylgalactosamine. Linkage unit of halobacterial glycosaminoglycan.

The Journal of biological chemistry ·Vol. 261 ·No. 3 ·1986-01-25 ·Pages 1020-4

Paul G, Lottspeich F, Wieland F

Abstract

The cell surface glycoprotein of Halobacteria contains two different types of sulfated saccharides: hexuronic acid-containing oligosaccharides linked to the protein via asparaginylglucose, and a serially repeated saccharide unit containing amino sugars that resembles the animal glycosaminoglycans. Here we report that 1) the sulfated repeating unit saccharide is linked to the cell surface glycoprotein via asparaginyl-N-acetylgalactosamine, 2) the amino acid sequence surrounding this linkage region is -Asn-Ala-Ser-, and thus in agreement with the acceptor sequence ASN-X-Thr(Ser) common to all eucaryotic N-glycosidically bound saccharides determined so far; 3) in addition to galactose, galacturonic acid, N-acetylglucosamine, and N-acetylgalactosamine, the methylated hexuronic acid 3-O-methylgalacturonic acid occurs as a stoichiometric constituent of the sulfated building block of the glycosaminoglycan chain.

MeSH Terms
Acetylgalactosamine/analogs & derivatives,analysis Amino Acids/analysis Asparagine/analogs & derivatives,analysis Carbohydrate Conformation Chromatography, High Pressure Liquid Galactosamine/analogs & derivatives Gas Chromatography-Mass Spectrometry Glycosaminoglycans/analysis Halobacterium/analysis Hydrolysis Sulfates/analysis
Chemicals
Amino Acids Glycosaminoglycans Sulfates asparaginyl-N-acetylgalactosamine Asparagine Galactosamine Acetylgalactosamine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Paul G
Lottspeich F
Wieland F
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1986-01-25
Pages
1020-4
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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