Characterization of the Lectin Purified from Canavalia ensiformis Shoots
2005
Roh, K.S. (Keimyung University, Daegu, Republic of Korea), E-mail: [email protected] | Park, N.Y. (Keimyung University, Daegu, Republic of Korea)
Lectin is a cell-agglutinating and carbohydrate-binding protein present in many plants. The lectin of Canavalia ensiformis shoot with specific affinity for D-glucose was purified by affinity chromatography using Sephadex G-100, and some of its biochemical characterizations were studied. Lectin was purified 8.87-fold and exhibited final specific activity of 225.74 units/mg protein with a 2.3% yield. SDS-PAGE analysis demonstrated that the purified shoot lectin exists as a tetramer of 102 kD, composed of two subunits with molecular weight of 29 and 22 kD.
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