Purification and molecular characterization of a novel mannose‐specific lectin from Dioclea reflexa hook seeds with inflammatory activity |
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| Authors: | Vanir R. Pinto‐Junior Jorge L. A. Correia Ronniery I. Pereira Francisco N. Pereira‐Junior Mayara Q. Santiago Vinicius J. S. Osterne Juliana C. Madeira João B. Cajazeiras Celso S. Nagano Plinio Delatorre Ana M. S. Assreuy Kyria S. Nascimento Benildo S. Cavada |
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| Affiliation: | 1. Laboratório de Moléculas Biologicamente Ativas (Biomol‐Lab), Department of Biochemistry and Molecular Biology, Federal University of Ceará, Fortaleza, CE, Brazil;2. Laboratório de Fisio‐Farmacologia da Inflama??o (LAFFIN), Institute of Biomedical Sciences, State University of Ceará, Fortaleza, CE, Brazil;3. Laboratório de Espectrometria de Massas aplicado a Proteínas (LEMAP), Federal University of Ceará, Fortaleza, CE, Brazil;4. Laboratório de Biologia Molecular Estrutural e Oncogenética (LBMEO), Department of Molecular Biology, Federal University of Paraíba, Jo?o Pessoa, PB, Brazil |
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| Abstract: | A novel lectin present in Dioclea reflexa seeds (DrfL) was discovered and described in this study. DrfL was purified in a single step by affinity chromatography in a Sephadex G‐50 column. The lectin strongly agglutinated rabbit erythrocytes and was inhibited by α‐methyl‐d ‐mannoside, d ‐mannose, and d ‐glucose. The hemagglutinating activity of DrfL is optimum at pH 5.0–7.0, stable up to 50 °C, and dependent on divalent cations. Similar to other lectins of the subtribe Diocleinae, the analysis by mass spectrometry indicated that DrfL has three chains (α, β, and γ) with masses of 25 562, 12 874, and 12 706 Da, respectively, with no disulfide bonds or glycosylation. DrfL showed inflammatory activity in the paw edema model and exhibited low cytotoxicity against Artemia sp. Copyright © 2015 John Wiley & Sons, Ltd. |
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| Keywords: | lectin Dioclea reflexa ESI mass spectrometry inflammatory activity |
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