• KSBB Journal
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• v.23 no.1
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• pp.48-53
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• 2008

Lectin was isolated from locular fluid of tomato by affinity chromatography using Sephadex G-200, and studied its some biochemical properties. SDS-PAGE of the isolated lectin revealed a tetramer composed of two identical subunits with molecular weights of 39 and 23 kDa. The isolated lectin was agglutinated by trypsin-treated human ABO type blood erythrocytes with similar potency, and the most activity of agglutination was found at B type blood erythrocyte. This lectin showed maximum thermal stability at $70^{\circ}C$, and was relatively stable to heat with the higher activity at $40-80^{\circ}C$. The optimal temperature and pH of this lectin were $50^{\circ}C$ and pH 7.0, respectively.

• KSBB Journal
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• v.25 no.3
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• pp.289-296
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• 2010

Lectins are carbohydrate-binding and a cell-agglutinating proteins, and are concerted with a plants defence mechanism. In particular, chitin-binding lectins in locular fluid of cherry tomato fruit seemed to have a role in defending plants against fungi. The antifungal activity using lectin isolated from locular fluid of cherry tomato fruit was measured in the plant pathogen Cladosporium cucumerinum, Monosporascus cannonballus, Fusarium oxysporum, and Rhizoctonia solani. Amoung the four strains, a potent antifungal activity was detected in Cladosporium cucumerinum and Monosporascus cannonballus, not in Fusarium oxysporum, and Rhizoctonia solani. The molecular weight of this lectin isolated as double protein bands by SDS-PAGE was calculated to be 87 kDa and 47 kDa from the relative mobilities compared with those of reference molecular weight markers. The isolated lectin agglutinated human red blood cells (A, B, AB, O) treated with trypsin, and the most activity was found at B. The optimal temperature of isolated lectin was at $30^{\circ}C$. For the thermal stability, lectin was stable at $20-80^{\circ}C$. The optimal pH of this lectin was at 7.2, and showed complete loss below pH 9.0.

• 한국생물공학회:학술대회논문집
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• 2005.10a
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• pp.551-552
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• 2005