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• W2134459887 abstract "Abstract Plasma membranes were purified from celery ( Apium graveolens L.) by two-phase partitioning and the UDP-glucose (1,3)-β-glucan (callose) synthase was solubilized with the detergent CHAPS. The techniques of moderate pressure anion exchange chromatography (FPLC), gel filtration chromatography, affinity chromatography on UDP-agarose and product-entrapment were then investigated as means for further purification. Enriched fractions were obtained by anion exchange chromatography in 0.1% CHAPS and 50 mM Tris-HCl (pH 7.5, spec. act., 568 nmol min −1 (mg prot.) −1 ), by affinity chromatography using UDP-agarose (1405 nmol min −1 (mg prot.) −1 ) and by product entrapment (914 nmol min −1 (mg prot.) −1 ). Fractions purified by anion exchange chromatography contained numerous polypeptides, however callose synthase purified by the affinity step yielded a silver-stained profile of six prominent polypeptides of 26.8, 30.5, 35, 41, 56 and 72 kDa. In the product-entrapped sample, the polypeptides of 41, 56 and 72 kDa incorporated [ 32 P]5N 3 UDP-Glc in a Ca 2+ -dependent manner, implying that these could play a role in the binding of UDP-Glc to the enzyme. The polypeptides at 26.8, 30.5, 35 and 72 kDa have also been observed in purified preparations from various other sources and could represent other components of the callose synthase complex." @default.
• W2134459887 created "2016-06-24" @default.
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• W2134459887 date "1992-01-01" @default.
• W2134459887 modified "2023-09-25" @default.
• W2134459887 title "Characterization of the UDP-glucose: (1,3)-β-glucan (callose) synthase from plasma membranes of celery: polypeptide profiles and photolabeling patterns of enriched fractions suggest callose synthase complexes from various sources share a common structure" @default.
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• W2134459887 doi "https://doi.org/10.1016/0168-9452(92)90158-i" @default.
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