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- W2079048699 abstract "Summary A carbohydrate-binding protein in the phloem exudate from Quercus robur L., Salix alba L. Tilia cordata Mill., and Ulmus glabra Huds. respectively was isolated by affinity chromatography on p-aminobenzyl-1-thio-N-acetyl-β-D-glucosaminide coupled to CH-sepharose 4 B. The yield of the purified proteins was in all the four cases about 10 μg/ml phloem exudate or about 10% of the total protein. So far as characterised, the four isolated lectins seemed to be identical. In disk electrophoresis at an alkaline ( p H 8.9) and acidic ( p H 4.3) pH the lectin appeared to be homogenous. Gel filtration revealed two components with a molecular weight of 30,000 and 5,000 D respectively. There was only one type of subunits (mol. wt. 5,000). The complex formation between the lectins and erythrocytes is inhibited by glycoproteins containing N-acetyl-D-glucosamine and by a partial hydrolysate of chitin, but not by simple sugars including the monomer N-acetyl-D-glucosamine." @default.
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- W2079048699 date "1980-01-01" @default.
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- W2079048699 title "Affinity Chromatography of Carbohydrate Binding Proteins in the Phloem Exudate from Several Tree Species" @default.
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- W2079048699 doi "https://doi.org/10.1016/s0015-3796(80)80090-4" @default.
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