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- W2070694674 abstract "Lectins are a class of proteins with specific carbohydrate-binding properties found in a wide variety of plants and animals. Gramineae lectins are presumably defense-related proteins in plants that exert their effect by binding to N-acetylglucosamine. Barley lectin is a vacuolar protein synthesized with an amino-terminal signal sequence for entering the secretory pathway and a carboxyl-terminal propeptide necessary for proper targeting to the vacuole. To analyze the three-dimensional structure of barley lectin with the carboxyl-terminal extension and to investigate whether the conversion of the prolectin into the mature molecule leads to a conformational change, the precursor and the mature forms of barley lectin were expressed in Escherichia coli. Both proteins accumulated in denatured form in inclusion bodies were solubilized in 8 M urea and renatured in a redox buffer system. Active pro- and mature barley lectins were purified to homogeneity by affinity chromatography." @default.
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- W2070694674 date "1992-12-01" @default.
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- W2070694674 title "Isolation and characterization of pro-Barley lectin expressed in Escherichia coli" @default.
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- W2070694674 doi "https://doi.org/10.1016/1046-5928(92)90068-8" @default.
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