Characterization of novel enzymic hemagglutinin isolated from Dregea volubilis

Abstract

A hemagglutinin was isolated from the fruit coats of the plant Dregea volubils to purity. The purified protein exhibited similar hemagglutination pattern with all the blood groups.  The hemagglutinin could agglutinate erythrocytes of other animals also except bullock. Molecular weight of the purified hemagglutinin was similar on SDS PAGE and sephadex G-75 gel filtration also. The hemagglutinating activity of the purified fraction was inhibited by α-D-glucose and α-D-mannose. Optimum pH was found to be 5.0 and optimum temperature stability was recorded to be at 45^oC, respectively. However, the hemagglutinin was stable from pH 4.0 to 7.0 and from temperature 5.0 to 55^oC, only. EDTA and 1, 10 phenanthrolein scavenged the metallic ion from the purified agglutinin, but Mg⁺⁺ was found to restore the activity to normal. The purified fraction exhibited α and β-glucosidase activity. Trypsin treatment of the purified fraction reduced the hemagglutinating and enzyme activity to nearly half. The purified fraction was found to be glycoprotein in nature and the carbohydrate moiety was detected to be GluNAc by TLC.