Isolation and Biochemical Characterization of a Galactoside Binding Lectin from <Emphasis Type="Italic">Bauhinia variegata</Emphasis> Candida (BvcL) Seeds |
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Authors: | José A Silva Daniela C S Damico Paulo A Baldasso Marcelo A Mattioli Flávia V Winck Leonardo F Fraceto José C Novello Sérgio Marangoni |
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Institution: | (1) Department of Biochemistry, Institute of Biology, State University of Campinas (UNICAMP), P. O. Box 6109, 13083-970 Campinas, SP, Brazil |
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Abstract: | A new lectin (BvcL) from seeds of a primitive Brazilian Caesalpinoideae, the Bauhinia variegata candida was purified and biochemical characterized. BvcL was isolated by gel filtration chromatography on Sephadex G75 and
affinity chromatography on immobilized d-lactose column. SDS-PAGE showed that BvcL under non-reducing condition presents two bands of 68 and 32 kDa and a single band
of 32 kDa in reducing condition. However, only one band was seen in native PAGE. The hemagglutination activity of BvcL was
not specific for any human blood group trypsin-treated erythrocytes. Carbohydrate inhibition analysis indicated that BvcL
is inhibited by lactose, galactose, galactosamine and other galactoside derivates. Amino acid analysis revealed a large content
of Ser, Gly, Thr, Asp and Glu and low concentrations of Met, Cys and His. Intrinsic fluorescence of BvcL was not significantly
affected by sugar binding galactose; and aromatic-region CD is unusually high for plant lectins. The N-terminal amino acid
sequence of 17 residues showed 90% sequential homology to galactose-specific legume lectins of the subfamily Caesalpinoideae. |
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Keywords: | Bauhinia variegata plant lectin seeds purification MALDI-TOF MS |
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