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      Molecular cloning of the lectin and a lectin-related protein from common Solomon's seal (Polygonatum multiflorum).

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          Abstract

          The most prominent protein of Polygonatum multiflorum (common Solomon's seal) rhizomes has been identified as a mannose-binding lectin. Analysis of the purified lectin demonstrated that it is a tetramer of four identical subunits of 14 kDa. Molecular cloning further revealed that the lectin from this typical Liliaceae species belongs to the superfamily of monocot mannose-binding proteins. Screening of cDNA libraries constructed with RNA isolated from buds, leaves and flowers of P. multiflorum also yielded cDNA clones encoding a protein, which contains two tandemly arranged domains with an obvious sequence homology to the mannose-binding lectins. Molecular modelling of the Polygonatum lectin and lectin-related protein indicated that the three-dimensional structure of both proteins strongly resembles that of the snowdrop lectin. In addition, this approach suggested that the presumed carbohydrate-binding sites of the lectin can accommodate a mannose residue whereas most of the carbohydrate-binding sites of the lectin-related protein cannot.

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          Author and article information

          Journal
          Plant Mol. Biol.
          Plant molecular biology
          0167-4412
          0167-4412
          Jun 1996
          : 31
          : 3
          Affiliations
          [1 ] Laboratory for Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Belgium.
          Article
          8790297

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