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• W2014339900 abstract "Abstract In contrast to microsomal membranes from suspension cultured cells undergoing primary wall synthesis which incorporated arabinose directly from UDP- β-L-arabinose into arabinan, membranes from cells treated with fungal elicitor catalysed the formation of a lipid oligosaccharide intermediate in the arabinosylation of an inducible M r 42 500 glycoprotein. These variations in the patterns and mechanism of arabinosylation observed between the cells in response to the differing stimuli were detected in both the kinetics of incorporation and the demonstration that the lipid oligosaccharide after purification on ion-exchange chromatography could act as primary donor for the glycoprotein and not polysaccharide. These results distinguish mechanisms for the transfers of arabinose onto glycoprotein and polysaccharide by enzyme systems known to be immunologically distinct. The fungal elicitor-induced M r 42 500 glycoprotein binds to thyrogolubulin- and fetuin-Sepharoses in a specific manner and this binding is prevented by chitin oligomers. The glycoprotein thus appears to be a carbohydrate-binding protein and the sugar specificity together with the demonstration of hydroxyproline residues in acid hydrolysates of the glycoprotein purified by affinity chromatography indicates a close similarity to the arabinosylated hydroxyproline-rich lectins of the Solanaceae which can function as bacterial agglutinins. The M r 42 500 glycoprotein which undergoes rapid transient induction also clearly differs from other extensin-like hydroxyproline-rich glycoproteins, arabinogalactan proteins and the characteristic bean seed-lectin, phytohaemagglutinin, in a number of properties." @default.
• W2014339900 created "2016-06-24" @default.
• W2014339900 creator A5030513641 @default.
• W2014339900 date "1986-07-01" @default.
• W2014339900 modified "2023-09-24" @default.
• W2014339900 title "Microsomal arabinosylation of polysaccharide and elicitor-induced carbohydrate-binding glycoprotein in french bean" @default.
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• W2014339900 doi "https://doi.org/10.1016/s0031-9422(00)81153-x" @default.
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