Please use this identifier to cite or link to this item: https://scholarhub.balamand.edu.lb/handle/uob/2450
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dc.contributor.authorRizk, Sandra E.en_US
dc.contributor.authorAbdel-Massih, Roulaen_US
dc.contributor.authorBaydoun, Elias A-H.en_US
dc.contributor.authorBrett, Cristopher T.en_US
dc.date.accessioned2020-12-23T09:13:34Z-
dc.date.available2020-12-23T09:13:34Z-
dc.date.issued2000-
dc.identifier.urihttps://scholarhub.balamand.edu.lb/handle/uob/2450-
dc.description.abstractNascent pectin and glucuronoarabinoxylan, synthesised in vitro by membrane-bound enzymes from etiolated pea (Pisum sativum L.) epicotyls, were found to bind to pea xyloglucan in a pH-dependent manner. The binding was maximum at low pH (3–4), and decreased to almost zero at pH 6. The binding was probably non-covalent and reached saturation within 5 min. Removal of the fucose residues of xyloglucan decreased the degree of binding. Removal by protease of the proteins attached to nascent pectin and glucuronoarabinoxylan greatly reduced the maximum binding and abolished the pH-dependence. The observed binding may be of considerable significance in the process of cell-wall assembly and in the control of cell extension.en_US
dc.format.extent6 p.en_US
dc.language.isoengen_US
dc.subjectBinding (pectin)en_US
dc.subjectGlucuronoarabinoxylanen_US
dc.subjectGlycoproteinen_US
dc.subjectPisumen_US
dc.subjectXyloglucanen_US
dc.subject.lcshPectinen_US
dc.titleProtein- and pH-dependent binding of nascent pectin and glucuronoarabinoxylan to xyloglucan in peaen_US
dc.typeJournal Articleen_US
dc.contributor.affiliationDepartment of Biologyen_US
dc.description.volume211en_US
dc.description.issue3en_US
dc.description.startpage423en_US
dc.description.endpage429en_US
dc.date.catalogued2017-10-31-
dc.description.statusPublisheden_US
dc.identifier.ezproxyURLhttp://ezsecureaccess.balamand.edu.lb/login?url=https://link.springer.com/article/10.1007/s004250000303en_US
dc.identifier.OlibID174657-
dc.relation.ispartoftextPlantaen_US
dc.provenance.recordsourceOliben_US
Appears in Collections:Department of Biology
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