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dc.contributor.authorWinterbourne, D J
dc.contributor.authorSchor, Ana M
dc.contributor.authorGallagher, John T
dc.date.accessioned2014-12-22T15:30:29Z
dc.date.available2014-12-22T15:30:29Z
dc.date.issued1983-09-15
dc.identifier.citationSynthesis of glycosaminoglycans by cloned bovine endothelial cells cultured on collagen gels. 1983, 135 (2):271-7 Eur J Biochemen
dc.identifier.issn0014-2956
dc.identifier.pmid6411471
dc.identifier.doi10.1111/j.1432-1033.1983.tb07648.x
dc.identifier.urihttp://hdl.handle.net/10541/337546
dc.description.abstractSulphated glycosaminoglycans have been analysed in cloned bovine aortic endothelial cells cultured on collagen gels after incubation with [3H]glucosamine and Na2(35)SO4. Radioactive products were analysed in the culture medium, in sequential collagenase and trypsin extracts of the cell monolayer and the associated extracellular matrix, and in the remaining viable cells. Heparan sulphate and chondroitin sulphate were found in each compartment: the heparan sulphate had a low degree of sulphation (approximately 0.4 N-sulphate and 0.2 O-sulphate groups per disaccharide unit on average). In the nitrous acid scission products of heparan sulphate, O-sulphated substituents were confined to disaccharide and tetrasaccharide fragments, indicating that local regions of the chain (which might be susceptible to excission by the platelet endoglycosidase) are highly sulphated. Only minor structural differences in heparan sulphate were observed between the various compartments. In contrast the chondroitin sulphate found in the collagenase extract had a higher iduronic acid content than corresponding material in the trypsin extract and the culture medium, indicating that collagenase and trypsin may extract glycosaminoglycans from different regions of the extracellular and pericellular matrix.
dc.language.isoenen
dc.rightsArchived with thanks to European journal of biochemistry / FEBSen
dc.subject.meshAnimals
dc.subject.meshCattle
dc.subject.meshChemical Phenomena
dc.subject.meshChemistry
dc.subject.meshChondroitin Sulfates
dc.subject.meshChromatography
dc.subject.meshClone Cells
dc.subject.meshCollagen
dc.subject.meshCulture Media
dc.subject.meshEndothelium
dc.subject.meshGels
dc.subject.meshGlycosaminoglycans
dc.subject.meshHeparitin Sulfate
dc.titleSynthesis of glycosaminoglycans by cloned bovine endothelial cells cultured on collagen gels.en
dc.typeArticleen
dc.contributor.departmentDepartment of biochemistry, St George's Hospital, Medical School, Londonen
dc.identifier.journalEuropean Journal of Biochemistryen
html.description.abstractSulphated glycosaminoglycans have been analysed in cloned bovine aortic endothelial cells cultured on collagen gels after incubation with [3H]glucosamine and Na2(35)SO4. Radioactive products were analysed in the culture medium, in sequential collagenase and trypsin extracts of the cell monolayer and the associated extracellular matrix, and in the remaining viable cells. Heparan sulphate and chondroitin sulphate were found in each compartment: the heparan sulphate had a low degree of sulphation (approximately 0.4 N-sulphate and 0.2 O-sulphate groups per disaccharide unit on average). In the nitrous acid scission products of heparan sulphate, O-sulphated substituents were confined to disaccharide and tetrasaccharide fragments, indicating that local regions of the chain (which might be susceptible to excission by the platelet endoglycosidase) are highly sulphated. Only minor structural differences in heparan sulphate were observed between the various compartments. In contrast the chondroitin sulphate found in the collagenase extract had a higher iduronic acid content than corresponding material in the trypsin extract and the culture medium, indicating that collagenase and trypsin may extract glycosaminoglycans from different regions of the extracellular and pericellular matrix.


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