Purification and erythrocyte-membrane perturbing activity of a ketose-specific lectin from seeds.

This study purified a hemagglutinating protein (MoL) from seed, and investigated its hemolytic activity. Molecular weight and stability of MoL were also determined. Modification of some amino acid residues was carried out and the effect on MoL hemagglutinating activity determined. Other investigated parameters are the effects of temperature, concentration, incubation period, pH, and sugars on the protein's hemagglutinating and hemolytic activities. The native and subunit molecular weights were estimated as 30 and 27.5 kDa respectively. Hemagglutinating activity of MoL was slightly inhibited by fructose and sucrose, stable at temperature up to 90°C and within pH range of 2-4. Modification of tryptophan and arginine residues resulted in partial loss of hemagglutinating activity. The hemolytic activity of MoL was concentration, temperature, pH, and time-dependent. The study concluded that MoL showed hemolytic (membrane-perturbing) activity in moderate acidic conditions. This suggests its potential exploitation in improved intracellular delivery of bioactive compounds.