Abstract

A novel lectin has been isolated from Ocimum Sanctum and purified to homogeneity by gel filtration chromatography. The protein eluted as a single symmetrical peak from a Biogel P-100 column with an apparent molecular mass of 66 kDa. The lectin had a specific agglutinating activity with human erythrocytes at a minimum concentration of 0.7µg/ml. The lectin was stable in the pH range 5-12 and at temperature less than or equal to 800C for 30 min. The lectin isolated from Ocimum Sanctum had shown highest agglutinating activity at pH 7 and 250C after one hour incubation. Of the various sugars tested, even at 1000 mM sugar concentration, no inhibition was observed. The isolated lectin was found to be a lactose-biding lectin and found to contain 2.6 mg/ml of total sugar and 9.3 mg/ml of total protein

Key words: Lectin, Blood group, Glycobiology, ELISA, Agglutination, Ocimum sanctum