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Characterization of the Lectin Purified from Canavalia ensiformis Shoots  

Roh, Kwang-Soo (Department of Biology, Keimyung University)
Park, Na-Young (Department of Biology, Keimyung University)
Publication Information
Biotechnology and Bioprocess Engineering:BBE / v.10, no.4, 2005 , pp. 334-340 More about this Journal
Abstract
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. The purified lectin was observed to agglutinate rabbit blood cell. The optimal temperature for the activity of this lectin was $40^{\circ}C$, and this lectin was relatively stable to heat with the highest activity at $50{\~}60^{\circ}C$. The maximal activity was observed at pH 7.2.
Keywords
Canavalia ensiformis shoot; hemagglutination activity; lectin; pH; thermal stability;
Citations & Related Records
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Times Cited By Web Of Science : 0  (Related Records In Web of Science)
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