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dc.contributor.authorGallagher, John T*
dc.contributor.authorWalker, Andrew*
dc.contributor.authorLyon, Malcolm*
dc.contributor.authorEvans, W H*
dc.date.accessioned2010-11-03T15:31:45Z
dc.date.available2010-11-03T15:31:45Z
dc.date.issued1988-03-15
dc.identifier.citationHeparan sulphate-degrading endoglycosidase in liver plasma membranes. 1988, 250 (3):719-26 Biochem. J.en
dc.identifier.issn0264-6021
dc.identifier.pmid3390139
dc.identifier.urihttp://hdl.handle.net/10541/114518
dc.description.abstractAn endoglycosidase is described in isolated liver plasma membranes that brings about a rapid and selective degradation of membrane-associated heparan sulphate, pre-labelled biosynthetically with Na2(35)SO4. The enzyme attacked mainly the polysaccharide chains of a hydrophobic membrane proteoglycan and it had little effect on a proteoglycan that could be displaced from the membranes with 1.0 M-NaCl. The highest activity was measured in the pH range 7.5-8.0, and the enzyme was almost completely inhibited below pH 5.5. Breakdown of susceptible polysaccharide chains was fast, being complete in 20-30 min. The major oligosaccharide fraction (Mr approx. 6000) produced by the enzyme was considerably smaller than the intact heparan sulphate chains. Enzyme activity was retained in membranes solubilized in 1% (v/v) Triton X-100. The high pH optimum and plasma-membrane association distinguish this enzyme from other heparan sulphate-degrading endoglycosidases that have acid pH optima and may be of lysosomal origin. A plasma-membrane endoglycosidase could modulate cellular interactions mediated by heparan sulphate, and/or release biologically active fragments of the polysaccharide from the cell periphery.
dc.language.isoenen
dc.subject.meshAnimals
dc.subject.meshCell Membrane
dc.subject.meshChromatography, Affinity
dc.subject.meshChromatography, Gel
dc.subject.meshGlucuronidase
dc.subject.meshGlycoside Hydrolases
dc.subject.meshHeparan Sulfate Proteoglycans
dc.subject.meshHeparitin Sulfate
dc.subject.meshHydrogen-Ion Concentration
dc.subject.meshLiver
dc.subject.meshPolysaccharides
dc.subject.meshProteochondroitin Sulfates
dc.subject.meshProteoglycans
dc.subject.meshRats
dc.titleHeparan sulphate-degrading endoglycosidase in liver plasma membranes.en
dc.typeArticleen
dc.contributor.departmentCancer Research Campaign Department of Medical Oncology, Christie Hospital, University of Manchester, U.K.en
dc.identifier.journalThe Biochemical Journalen
html.description.abstractAn endoglycosidase is described in isolated liver plasma membranes that brings about a rapid and selective degradation of membrane-associated heparan sulphate, pre-labelled biosynthetically with Na2(35)SO4. The enzyme attacked mainly the polysaccharide chains of a hydrophobic membrane proteoglycan and it had little effect on a proteoglycan that could be displaced from the membranes with 1.0 M-NaCl. The highest activity was measured in the pH range 7.5-8.0, and the enzyme was almost completely inhibited below pH 5.5. Breakdown of susceptible polysaccharide chains was fast, being complete in 20-30 min. The major oligosaccharide fraction (Mr approx. 6000) produced by the enzyme was considerably smaller than the intact heparan sulphate chains. Enzyme activity was retained in membranes solubilized in 1% (v/v) Triton X-100. The high pH optimum and plasma-membrane association distinguish this enzyme from other heparan sulphate-degrading endoglycosidases that have acid pH optima and may be of lysosomal origin. A plasma-membrane endoglycosidase could modulate cellular interactions mediated by heparan sulphate, and/or release biologically active fragments of the polysaccharide from the cell periphery.


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