V. O. Antonyuk^1,2, L. V. Panchak^1,2, M. O. Starykovych¹, R. S. Stoika¹

¹Institute of Cell Biology, National Academy of Sciences of Ukraine, Lviv, Ukraine;
²Danylo Halytsky Lviv National Medical University, Ukraine;
e-mail: antonyuk@meduniv.lviv.ua

A new lectin was purified from the daylily (Hemerocallis fulva L.) with the yield of approximately 10 mg per kg of fresh plant rhizome. The purification procedure was based on application of the affinity chromathography on the column with yeast mannan and the ion-exchange chromatography on the column with DEAE-Toyopearl. The lectin possessed low affinity for α-methyl-D-mannopyranoside, D-fructose, D-turanose and 2-acetamido-D-galactopyranose and hight affinity for the yeast mannan. The lectin bound with greatly less affinity for the mannose-containig glycoproteins, such as ovoalbumin, ovomucoid and horseradish peroxidase. According to the results of electrophoresis in 20% DSNa-PAGE, the lectin consists of subunits of 12 kDa molecular weight. According to the results of gel-chromatography on the Toyopearl HW-55, the lectin’s molecular weight is 48 kDa. It agglutinated rabbit erythrocytes very well, while rat and guinea-pig erythrocytes were agglutinated worse, and human erythrocytes were not agglutinated at all.  Lectin’s dialysis against 1% EDTA or heating to 60 ºC for 60 min did not stop its hemagglutinating activity.