Heparan Sulphate (HS) Oligoaccharides
Excised by Specific Enzymes
Analysis of HS domain Organisation
Heparan Sulphate (HS) is a near-universal co-receptor for many growth factors and morphogenic proteins; it has a complex domain organisation of alternating high and low sulphated regions (Fig 1) in which the various patterns of modification by sulphation by and epimerisation create considerable structural diversity designed for selective binding to its many client proteins.
We offer two classes of Heparan Sulphate Oligosaccharides (HS-oligos) prepared by:
1. Heparinase III digestion of the low sulphated regions of HS resulting in oligosaccharides rich in the Heparinase III resistant high-sulphation domains (S-domains)
2. Heparinase I digestion of the S-domains of HS resulting in oligosaccharides made from the Heparinase I resistant regions of low/intermediate sulphation.
The HS-oligos in the enzyme digests were separated by high resolution gel filtration and the molecular size profiles of the individual peaks assesed on Superdex S-75 hplc. Although substantially homogeneous on S-75 the HS-oligos in each size class will contains sequences that vary in composition and there may be some limited overlap with oligos in adjacent size groups.