Biochemical characterisation of lectin from Indian hyacinth plant bulbs with potential inhibitory action against human cancer cells

This work describes purification and characterisation of a monocot mannose-specific lectin from Hyacinth bulbs. The purified lectin has a molecular mass of ∼30 kDa in reducing as well as in non-reducing SDS-PAGE. In hydrodynamic studies by Dynamic Light Scattering (DLS) showed that purified lectin was monomeric in nature with a molecular size of 2.38 ± 0.03 nm. Agglutination activity of purified lectin was confirmed by rabbit erythrocytes and its agglutination activity was inhibited by d-mannose and a glycoprotein (ovalbumin). Glycoprotein nature of purified lectin was confirmed by Periodic Acid Schiff’s (PAS) stain. Purified lectin showed moderate pH and thermal stability by retaining hemagglutination activity from pH 6–8 and temperature up to 60 °C. It also suppressed the growth of human colon cancer cells (Caco-2) and cervical cancer cells (HeLa) with IC50 values of 127 μg/mL and 158 μg/mL respectively, after 24-h treatment. Morphological studies of treated cells (Caco-2 and HeLa) with hyacinth lectin by AO/EB dual staining indicated that purified lectin is capable of inducing apoptosis.