Crataeva tapia bark lectin is an affinity adsorbent and insecticidal agent
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2012-02-01
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Sousa de Araujo, Regina Maria
Ferreira, Rodrigo da Silva [UNIFESP]
Napoleao, Thiago Henrique
Carneiro-da-Cunha, Maria das Gracas
Breitenbach Barroso Coelho, Luana Cassandra
Santos Correia, Maria Tereza dos
Oliva, Maria Luiza Vilela [UNIFESP]
Guedes Paiva, Patricia Maria
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Hemagglutinating activity has been associated to presence of lectin, carbohydrate-binding proteins. in this work Crataeva tapia bark lectin (CrataBL) was purified in milligram quantities (28 mg per g of bark) by ion exchange chromatography. the lectin was thermo-stable, ion-independent and N-terminal sequence analysis demonstrated similarity with miraculin and miraculin-like proteins (plant defensive proteins). Glycosylated nature of CrataBL was revealed using glycoprotein staining (periodic acid-Schiff's reagent), positive for polypeptides of apparent molecular masses 21 and 40 kDa on SOS-PAGE. Gel diffusion assay showed that glucose/mannose isolectins from Cratylia mollis recognized CrataBL glycan moiety. CrataBL hemagglutinating activity was inhibited by glycoproteins and CrataBL immobilized on cyanogen bromide-activated sepharose 4B (1 mL) bound 0.54 mg of glycoprotein (casein, fetuin and ovalbumin) per cycle. CrataBL was an insecticide agent against Nasutitermes corniger workers (termite that attack woods) with LC50 of 0.475 mg mL(-1) for 6 days. (C) 2011 Elsevier Ireland Ltd. All rights reserved.
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Plant Science. Clare: Elsevier B.V., v. 183, p. 20-26, 2012.