BUL: A novel lectin from Bauhinia ungulata L. seeds with fungistatic and antiproliferative activities |
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| Affiliation: | 1. Department of Biochemistry and Molecular Biology, Federal University of Ceará, 60455-760 Fortaleza, Ceará, Brazil;2. Department of Chemistry, University of Warwick, Coventry CV4 7AL, UK;3. Department of Organic and Inorganic Chemistry, Federal University of Ceará, 60455-900 Fortaleza, Ceará, Brazil;4. Department of Fishing and Engineering, Federal University of Ceará, 60455-900 Fortaleza, Ceará, Brazil;1. Departamento de Bioquímica, Universidade Federal de São Paulo, Rua Três de Maio 100, 04044-020 São Paulo, SP, Brazil;2. Departamento de Biofísica, Universidade Federal de São Paulo, Rua Três de Maio 100, 04044-020 São Paulo, SP, Brazil;3. Instituto de Pesquisas Jardim Botânico do Rio de Janeiro, Rua Pacheco Leão 915, 22460-030 Rio de Janeiro, RJ, Brazil;4. Departamento de Bioquímica, Universidade Federal de Pernambuco, Avenida Professor Moraes Rego s/n, 50670-910 Recife, PE, Brazil |
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| Abstract: | ![]()
A new galactose-binding lectin, termed BUL, has been purified from seeds of Bauhinia ungulata L. (Caesalpinoideae) by precipitation with solid ammonium sulfate followed by agarose–lactose affinity chromatography. B. ungulata lectin strongly agglutinated rabbit erythrocytes, both native and treated with proteolytic enzymes, and was inhibited by d-galactose and d-galactose-derived sugars, especially N-acetyl-d-galactosamine. BUL was shown to be a stable glycoprotein, maintaining its hemagglutinating activity after incubation at wide ranges of temperature and pH, but not after incubation with EDTA. By SDS-PAGE analysis, purified BUL showed an electrophoretic profile consisting of a single band with apparent molecular mass of 30 kDa. BUL showed intrinsic fluorescence typical of folded globular proteins, and CD spectra of lectin in the native state showed a predominance of β-sheet secondary structure. The N-terminal amino acid sequence of 19 residues showed a high sequential similarity to other galactose-specific lectins from the Bauhinia genus. In addition, BUL showed antifungal activity against phytopathogenic species and showed in vitro antiproliferative activity against the HT-29 cell line of human colon adenocarcinoma in a dose-dependent manner. |
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| Keywords: | Lectin Fungistatic and antiproliferative activities |
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