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  • Title: Sialic acid-binding dwarf elder four-chain lectin displays nucleic acid N-glycosidase activity.
    Author: Iglesias R, Citores L, Ferreras JM, Pérez Y, Jiménez P, Gayoso MJ, Olsnes S, Tamburino R, Di Maro A, Parente A, Girbés T.
    Journal: Biochimie; 2010 Jan; 92(1):71-80. PubMed ID: 19799962.
    Abstract:
    Sialic acid-binding dwarf elder agglutinin (SEA) present only in rhizomes of the medicinal plant Sambucus ebulus L., was found to be a tetrameric glycoprotein consisting of two covalently-associated dimers of an enzymic A chain with rRNA N-glycosidase activity (EC 3.2.2.22) linked to a B chain with agglutinin properties. The lectin inhibited protein synthesis by a cell-free system and depurinated ribosomes. Cloning of the corresponding gene and molecular modeling of the deduced amino acid sequence demonstrated that SEA has a three-dimensional structure which resembles that reported for other two tetrameric type 2 RIPs from Sambucus (SNAI and SSA). The lectin agglutinated red blood cells and displayed sugar affinity for sialic acid residues apart from d-galactose, binding to the mucin-producing gut goblet cells. Since sialic acid is present in animal cells, especially in epithelial lining gut cells, but not in plants, SEA could play a role in the defense against insect attack. The nucleotide sequence reported in this paper has been submitted to the GenBank nucleotide database under accession number AM981401.
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