Structural differences and the presence of unsubstituted amino groups in heparan sulphates from different tissues and species

Toshihiko Toida, Hisao Yoshida, Hidenao Toyoda, Ichiro Koshiishi, Toshio Imanari, Ronald E. Hileman, Jonathan R. Fromm, Robert J. Linhardt

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This study presents a comparison of heparan sulphate chains isolated from various porcine and bovine tissues. H-NMR spectroscopy (500 MHz) was applied for structural and compositional studies on intact heparan sulphate chains. After enzymic digestion of heparan sulphate using heparin lyase I (EC II and III (EC, the compositions of unsaturated disaccharides obtained were determined by analytical capillary electrophoresis. Correlations between the N-sulphated glucosamine residues and O-sulphation and between iduronic acid content and total sulphation were discovered using the data obtained by NMR and disaccharide analysis. Heparan sulphate chains could be classified into two groups based on the sulphation degree and the iduronic acid content. Heparan sulphate chains with a high degree of sulphation possessed also a significant number of iduronic acid residues and were isolated exclusively from porcine brain, liver and kidney medulla. The presence and amount of N-unsubstituted glucosamine residues (GlcNp) was established in all of the heparan sulphates examined. The structural context in which this residue occurs was demonstrated to be: high sulphation domain → 4)-β-D-GlcAp-(1 → 4)-α-D-GlcNp-(1 → 4)-β-D-GlcAp-(1→ low sulphation domain (where GlcNp is 2-amino-2-deoxyglucopyranose, and GlcAp is glucopyranosyluronic acid), based on the isolation and characterization of a novel, heparin lyase III-derived, GlcNp containing tetrasaccharide and hexa-saccharide. The results presented suggest that structural differences may play a role in important biological events controlled by heparan sulphate in different tissues.

Original languageEnglish
Pages (from-to)499-506
Number of pages8
JournalBiochemical Journal
Issue number2
StatePublished - 1 Mar 1997
Externally publishedYes


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