Purification and primary structure of a mannose/glucose‐binding lectin from Parkia biglobosa Jacq. seeds with antinociceptive and anti‐inflammatory properties |
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Authors: | Helton C Silva Alfa U Bari Bruno Anderson M Rocha Kyria S Nascimento Edson L Ponte Alana F Pires Plínio Delatorre Edson H Teixeira Henri Debray Ana Maria S Assreuy Celso S Nagano Benildo S Cavada |
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Institution: | 1. BioMol‐Group, Department of Biochemistry and Molecular Biology, Federal University of Ceará, , 60440‐970 Fortaleza, CE, Brazil;2. BioMol‐Group, Institute of Biomedical Sciences, State University of Ceará, , Fortaleza, CE, Brazil;3. BioMol‐Group, Department of Molecular Biology, Federal University of Paraíba, , Jo?o Pessoa, PB, Brazil;4. BioMol‐Group, Department of Pathology and Legal Medicine, Faculty of Medicine, Federal University of Ceará, , Fortaleza, CE, Brazil;5. University of Science and Technology of Lille, , Lille, France;6. BioMol‐Group, Department of Fishing Engineering, Federal University of Ceará, , Fortaleza, CE, Brazil |
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Abstract: | Parkia biglobosa (subfamily Mimosoideae), a typical tree from African savannas, possess a seed lectin that was purified by combination of ammonium sulfate precipitation and affinity chromatography on a Sephadex G‐100 column. The P. biglobosa lectin (PBL) strongly agglutinated rabbit erythrocytes, an effect that was inhibited by d ‐mannose and d ‐glucose‐derived sugars, especially α‐methyl‐d ‐mannopyranoside and N‐acetyl‐d ‐glucosamine. The hemagglutinating activity of PBL was maintained after incubation at a wide range of temperature and pH and also was independent of divalent cations. By sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis, PBL exhibited an electrophoretic profile consisting of a single band with apparent molecular mass of 45 kDa. An analysis using electrospray ionization–mass spectrometry indicated that purified lectin possesses a molecular average mass of 47 562 ± 4 Da, and the analysis by gel filtration showed that PBL is a dimer in solution. The complete amino acid sequence of PBL, as determined using tandem mass spectrometry, consists of 443 amino acid residues. PBL is composed of a single non‐glycosylated polypeptide chain of three tandemly arranged jacalin‐related domains. Sequence heterogeneity was found in six positions, indicating that the PBL preparations contain highly homologous isolectins. PBL showed important antinociceptive activity associated to the inhibition of inflammatory process. Copyright © 2013 John Wiley & Sons, Ltd. |
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Keywords: | lectin Parkia biglobosa subfamily Mimosoideae |
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