B. Joshi et al., PURIFICATION AND CHARACTERIZATION OF A LECTIN FROM XANTHOMONAS-CAMPESTRIS NCIM-5028, Canadian journal of microbiology, 42(6), 1996, pp. 609-612
A lectin was isolated from culture filtrates of Xanthomonas campestris
NCIM 5028, by a simple procedure of hydrophobic chromatography on phe
nyl-Sepharose after ammonium sulphate precipitation. The lectin was a
heterodimer, with subunit molecular masses of 30 000 and 28 000. Gel f
iltration on S-300 column, calibrated with markers, showed its molecul
ar 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.