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Glycobiology Advance Access published online on October 30, 2002
Glycobiology, doi:10.1093/glycob/cwg006
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Submitted on May 24, 2002
Revised on August 14, 2003
Accepted on August 21, 2002

© 2002 Oxford University Press

ORIGINAL ARTICLES

Heparin Sequencing

Sally E. Stringer 1*, Balbant S. Kandola 1, David A. Pye 1, John T. Gallagher 2

1 Drug Development Group, University of Manchester, Paterson Institute for Cancer Research, Christie Hospital NHS Trust, Manchester. M20 4BX. UK
2 Medical Oncology Department, University of Manchester, Paterson Institute for Cancer Research, Christie Hospital NHS Trust, Manchester. M20 4BX. UK

* To whom correspondence should be addressed. E-mail: sallyelizabethstringer{at}yahoo.co.uk.

Abstract

Heparin is a highly sulphated glycosaminoglycan widely used as an anticoagulant. Modifications in its relatively uniform structure appear to be key to its recognition and modulation of serine proteases, growth factors, chemokines and extracellular proteins, as has been most clearly demonstrated in the antithrombin binding site. We have sequenced the major oligosaccharides released from mastocytoma heparin by partial nitrous acid using a highly sensitive technique tailored for sequencing of metabolically radiolabeled heparin. It utilises partial nitrous acid cleavage to allow simultaneous sequencing of the internal components of the oligosaccharide under investigation by specific lysosomal exoenzymes. Sequencing revealed that whilst the majority of the heparin disaccharides are N, 2-O- and 6-O-sulphated, the less sulphated disaccharides (lacking 2-O- or 6-O-sulphates) seem to be spaced out along the chain. The technique described may be particularly useful for characterising heparin from novel sources, such as the glial progenitor cells and Ascidia as well as for sequencing protein binding sites.


Key words: Heparin, sequencing, proteoglycan, glycosaminoglycan, exoenzymes
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