Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/197621
Type: Artigo de periódico
Title: Isolation And Biochemical Characterization Of A Galactoside Binding Lectin From Bauhinia Variegata Candida (bvcl) Seeds.
Author: Silva, José A
Damico, Daniela C S
Baldasso, Paulo A
Mattioli, Marcelo A
Winck, Flávia V
Fraceto, Leonardo F
Novello, José C
Marangoni, Sérgio
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.
Subject: Amino Acid Sequence
Animals
Bauhinia
Electrophoresis, Gel, Two-dimensional
Galectins
Humans
Molecular Sequence Data
Plant Lectins
Rabbits
Seeds
Sequence Alignment
Spectrometry, Mass, Matrix-assisted Laser Desorption-ionization
Rights: fechado
Identifier DOI: 10.1007/s10930-006-9061-0
Address: http://www.ncbi.nlm.nih.gov/pubmed/17203390
Date Issue: 2007
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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