Purification and Partial Characterization of a Lectin from Canavalia Grandiflora Benth. Seeds

Author(s): V. M. Ceccatto, B. S. Cavada, E. P. Nunes, N. A.P. Nogueira, M. B. Grangeiro, F.B. M.B. Moreno, E. H. Teixeira, A. H. Sampaio, M. A.O. Alves, M. V. Ramos, J. J. Calvete, T. B. Grangeiro

Journal Name: Protein & Peptide Letters

Volume 9 , Issue 1 , 2002

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A D-glucose / D-mannose specific lectin from seeds of Canavalia grandiflora (ConGF) was purified by affinity chromatography on Sephadex G-50. By SDS-PAGE ConGF yielded three protein bands with apparent molecular masses of 29-30 kDa (α chain), 16-18 kDa (β fragment) and 12-13 kDa (γ fragment), like other related lectins from the genus Canavalia (Leguminosae). ConGF strongly agglutinates rabbit erythrocytes, has a high content of ASP and SER, and its N-terminal sequence (30 residues) is highly similar to the sequences of other related lectins from subtribe Diocleinae.

Keywords: Canavalia grandiflora, (Leguminosae family), Papilionoideae, N-terminal amino acid, D-glucopyranoside, subtribe Diocleinae

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Article Details

Year: 2002
Page: [67 - 73]
Pages: 7
DOI: 10.2174/0929866023409002

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