Purification and characterization of a cell-surface lectin (Lectin II) from Agrobacterium radiobacter NCIM 2443.
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.
Syed
F B
FB
Division of Biochemical Sciences, National Chemical Laboratory, Pune, India.
Joshi
B N
BN
SivaRaman
H
H
Khire
J M
JM
Khan
M I
MI
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*
D000596:Amino Acids; D001426:Bacterial Proteins; D006023:Glycoproteins; D037102:Lectins; D009005:Monosaccharides; D011134:Polysaccharides