A Novel Hemagglutinin from Seeds of Dregea volubilis

A novel hemagglutinating protein was isolated from seeds of wild medicinal plant Dregea volubilis. The hemagglutinin was purified by conventional purification procedure followed by affinity chromatography on cross linked starch entrapped in agarose beads. The homogeneous preparation on simple PAGE and SDSPAGE expressed little low molecular weight. Mr detected on SDS PAGE was found to be 16 kD and on sephadex G75 it was recorded as 15.48 kD. Optimum pH for agglutinating activity was between pH 4 to7. Optimum temperature for activity was 45o C but the protein was stable from 5 to 55o C. Activity of purified hemagglutinin of D. volubilis seeds was activated by Mg++. The hemagglutinin was identified as glycoprotein in nature with enzymic activity and antiproliferting property towards CPA47 cells.