Onyeyirichi I., Mario I.H., Sani I., Joshua O., Ogechi N.
Biochemistry Division, Basic Research Department, National Research Institute for Chemical Technology, Basawa, Zaria, Kaduna State, Nigeria; Department of Biochemistry, Faculty of Science, Ahmadu Bello University Zaria, Kaduna State, Nigeria; Petrochemica
Onyeyirichi, I., Biochemistry Division, Basic Research Department, National Research Institute for Chemical Technology, Basawa, Zaria, Kaduna State, Nigeria; Mario, I.H., Department of Biochemistry, Faculty of Science, Ahmadu Bello University Zaria, Kaduna State, Nigeria; Sani, I., Department of Biochemistry, Faculty of Science, Ahmadu Bello University Zaria, Kaduna State, Nigeria; Joshua, O., Petrochemical Division, National Research Institute for Chemical Technology, Basawa, Zaria, Kaduna State, Nigeria; Ogechi, N., Biochemistry Division, Basic Research Department, National Research Institute for Chemical Technology, Basawa, Zaria, Kaduna State, Nigeria
Lectin from Erythrophleum suaveolens stem bark was partially purified and evaluated in terms of its haemagglutination activity. Ground, dried stem bark of Erythrophleum suaveolens was extracted by aqueous method and theprotein extract was concentrated in 20-90% saturation. The ammonium sulfate precipitate was subjected to gel filtration chromatography using Sephadex G-75 resin and fractions were tested for haemagglutination activity. The two fractions obtained with the highest hemmaglutinating activity were further subjected separately to ion-exchange chromatography using Sp- Sephadex C-50 resin. Isolated lectins were found to agglutinate chicken erythrocytes; fractions from gel filtration chromatography showed haemagglutinating activity of 0.1 HU/μL and 0.091 HU/μL, while the ion exchange fractions showed haemagglutinating activity of 0.05 HU/μL and all were stable at the temperature range of 30-60°C and pH range of 3-7. The carbohydrate content of the crude extract, Gel I, Gel II, Ion I and Ion II fractions were 0.04 %, 0.04 %, 0.03 %, 0.02 %, respectively. The crude and purified lectins inhibited agglutination in the presence of mannose and Nacetyl- glucoseamine sugars and showed five bands at positions 38kDa, 28kDa, 26kDa, 11kDa and 9kDa on a SDS-PAGE electrophoregram.
lectin; mannose; n acetylglucosamine; agglutination test; animal cell; article; bark; carbohydrate analysis; chicken; concentration response; controlled study; drug isolation; drug purification; drug screening; erythrocyte; erythrophleum suaveolens; Fabaceae; hemagglutination; nonhuman; pH; phytochemistry; plant stem; temperature sensitivity; tree