2.50
Hdl Handle:
http://hdl.handle.net/10541/82394
Title:
Heparin sequencing.
Authors:
Stringer, Sally E; Kandola, Balbant S; Pye, David A; Gallagher, John T
Abstract:
Heparin is a highly sulfated 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 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 utilizes partial nitrous acid cleavage to allow simultaneous sequencing of the internal components of the oligosaccharide under investigation by specific lysosomal exoenzymes. Sequencing revealed that although the majority of the heparin disaccharides are N-, 2-O-, and 6-O-sulfated, the less sulfated disaccharides (lacking 2-O- or 6-O-sulfates) seem to be spaced out along the chain. The technique may be particularly useful for characterizing heparin from novel sources, such as the glial progenitor cells and Ascidia, as well as for sequencing protein binding sites.
Affiliation:
Drug Development Group, Paterson Institute for Cancer Research, Christie Hospital NHS Trust, Manchester M20 4BX, UK. sallyelizabethstringer@yahoo.co.uk
Citation:
Heparin sequencing. 2003, 13 (2):97-107 Glycobiology
Journal:
Glycobiology
Issue Date:
Feb-2003
URI:
http://hdl.handle.net/10541/82394
DOI:
10.1093/glycob/cwg006
PubMed ID:
12626406
Type:
Article
Language:
en
ISSN:
0959-6658
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorStringer, Sally E-
dc.contributor.authorKandola, Balbant S-
dc.contributor.authorPye, David A-
dc.contributor.authorGallagher, John T-
dc.date.accessioned2009-09-23T15:23:07Z-
dc.date.available2009-09-23T15:23:07Z-
dc.date.issued2003-02-
dc.identifier.citationHeparin sequencing. 2003, 13 (2):97-107 Glycobiologyen
dc.identifier.issn0959-6658-
dc.identifier.pmid12626406-
dc.identifier.doi10.1093/glycob/cwg006-
dc.identifier.urihttp://hdl.handle.net/10541/82394-
dc.description.abstractHeparin is a highly sulfated 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 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 utilizes partial nitrous acid cleavage to allow simultaneous sequencing of the internal components of the oligosaccharide under investigation by specific lysosomal exoenzymes. Sequencing revealed that although the majority of the heparin disaccharides are N-, 2-O-, and 6-O-sulfated, the less sulfated disaccharides (lacking 2-O- or 6-O-sulfates) seem to be spaced out along the chain. The technique may be particularly useful for characterizing heparin from novel sources, such as the glial progenitor cells and Ascidia, as well as for sequencing protein binding sites.en
dc.language.isoenen
dc.subjectCultured Tumour Cellsen
dc.subject.meshAnimals-
dc.subject.meshCarbohydrate Sequence-
dc.subject.meshChromatography, High Pressure Liquid-
dc.subject.meshElectrophoresis, Polyacrylamide Gel-
dc.subject.meshHeparin-
dc.subject.meshIduronidase-
dc.subject.meshMolecular Sequence Data-
dc.subject.meshNitrous Acid-
dc.subject.meshOligosaccharides-
dc.subject.meshParticle Size-
dc.subject.meshSequence Analysis-
dc.subject.meshSulfatases-
dc.subject.meshTumor Cells, Cultured-
dc.titleHeparin sequencing.en
dc.typeArticleen
dc.contributor.departmentDrug Development Group, Paterson Institute for Cancer Research, Christie Hospital NHS Trust, Manchester M20 4BX, UK. sallyelizabethstringer@yahoo.co.uken
dc.identifier.journalGlycobiologyen

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