title: Purification and characterization of a cell-surface lectin (Lectin II) from Agrobacterium radiobacter NCIM 2443.
abstract: A lectin was isolated from Agrobacterium radiobacter cell surface and purified. It is a monomer of 40 kDa as shown by SDS-PAGE. The lectin has a pI of 9.15 and amino acid composition of the lectin shows that 44% of the amino acids are hydrophobic. The lectin agglutinates rabbit erythrocytes but does not agglutinate human erythrocytes. It does not show specificity for monosaccharides except for D-glucosamine. Fetuin and its N-linked glycopeptide also inhibit the activity of the lectin but greater inhibition is shown by locust bean gum and Nicotiana tobaccum (tobacco) tissue extracts.
authors: Division of Biochemical Sciences, National Chemical Laboratory, Pune, India.
authors: F B
authors: FB
authors: Syed
authors: B N
authors: BN
authors: Joshi
authors: H
authors: H
authors: SivaRaman
authors: J M
authors: JM
authors: Khire
authors: M I
authors: MI
authors: Khan
mesh_terms: D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins / Q000302:isolation & purification*; D006023:Glycoproteins / Q000378:metabolism; D006384:Hemagglutination; D037102:Lectins / Q000302:isolation & purification*; D009005:Monosaccharides / Q000378:metabolism; D011134:Polysaccharides / Q000378:metabolism; D011485:Protein Binding; D012231:Rhizobium / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D001426:Bacterial Proteins; D006023:Glycoproteins; D037102:Lectins; D009005:Monosaccharides; D011134:Polysaccharides