Abstract
Lectin is a cell-agglutinating and carbohydrate-binding protein present in many plants. The lectin ofCanavalia ensiformis shoot with specific affinity ford-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. The purified lectin was observed to agglutinate rabbit blood cell. The optimal temperature for the activity of this lectin was 40°C, and this lectin was relatively stable to heat with the highest activity at 50∼60°C. The maximal activity was observed at pH 7.2.
Published Version
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