Purification and characterization of a lectin from Xanthomonas campestris NCIM 5028

A lectin was isolated from culture filtrates of Xanthomonas campestris NCIM 5028, by a simple procedure of hydrophobic chromatography on phenyl-Sepharose after ammonium sulphate precipitation. The lectin was a heterodimer, with subunit molecular masses of 30 000 and 28 000. Gel filtration on S-300 column, calibrated with markers, showed its molecular mass to be approximately 70 000. Its isoelectric point was 7.2. The agglutination of the rabbit erythrocytes by the lectin was inhibited by fetuin glycopeptides and host plant (Brassica oleracea) extracts.Key words: Xanthomonas campestris, lectin, purification.

[1]  A. Lachke,et al.  Purification of α-l-arabinofuranosidase using a single-column mini-scale isoelectric focusing unit , 1995 .

[2]  I. Chet,et al.  A newly isolated lectin from the plant pathogenic fungus Sclerotium rolfsii: purification, characterization and role in mycoparasitism. , 1994, Microbiology.

[3]  J. L. Wang,et al.  Carbohydrate binding activities of Bradyrhizobium japonicum: unipolar localization of the lectin BJ38 on the bacterial cell surface. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[4]  M. Monsigny,et al.  Characterization of an Agrobacterium tumefaciens lectin. , 1991, Glycobiology.

[5]  J. L. Wang,et al.  Carbohydrate binding activities of Bradyrhizobium japonicum. I. Saccharide-specific inhibition of homotypic and heterotypic adhesion , 1990, The Journal of cell biology.

[6]  D. Coplin,et al.  Molecular genetics of extracellular polysaccharide biosynthesis in vascular phytopathogenic bacteria. , 1990, Molecular plant-microbe interactions : MPMI.

[7]  N. Sharon.  Bacterial lectins, cell‐cell recognition and infectious disease , 1987, FEBS letters.

[8]  R. Townsend,et al.  Binding of N-linked bovine fetuin glycopeptides to isolated rabbit hepatocytes: Gal/GalNAc hepatic lectin discrimination between Gal beta(1,4)GlcNAc and Gal beta(1,3)GlcNAc in a triantennary structure. , 1986, Biochemistry.

[9]  D. Northcote,et al.  Cell-cell recognition of host surfaces by pathogens. The adsorption of maize (Zea mays) root mucilage by surfaces of pathogenic fungi. , 1986, The Biochemical journal.

[10]  N. Sharon,et al.  Soybean agglutinin--a plant glycoprotein. Structure of the carboxydrate unit. , 1978, The Journal of biological chemistry.

[11]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[12]  Oliver H. Lowry,et al.  Protein measurement with the Folin phenol reagent. , 1951, The Journal of biological chemistry.

[13]  T. Denny,et al.  Genetic evidence that extracellular polysaccharide is a virulence factor of Pseudomonas solanacearum , 1991 .

[14]  G. Smit,et al.  Roles of Lectin in the Rhizobium -Legume Symbioses , 1991 .

[15]  G. Gaard,et al.  Interaction of bacteria and host cell walls: its relation to mechanisms of induced resistance , 1977 .

[16]  J. Brandts,et al.  High precision capillary viscometry. , 1972, Methods in enzymology.

[17]  G. Stevens.  [6] Preparation and properties of cellulose, hemicellulose, and cellobiose , 1957 .

[18]  F. Smith,et al.  COLORIMETRIC METHOD FOR DETER-MINATION OF SUGAR AND RELATED SUBSTANCE , 1956 .