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

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

Volume: 9 Issue: 1

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 and T. B. Grangeiro

Affiliation:

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

Abstract: 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.

Cite this article as:

Ceccatto M. V., Cavada S. B., Nunes P. E., Nogueira A.P. N., Grangeiro B. M., Moreno M.B. F.B., Teixeira H. E., Sampaio H. A., Alves A.O. M., Ramos V. M., Calvete J. J. and Grangeiro B. T., Purification and Partial Characterization of a Lectin from Canavalia Grandiflora Benth. Seeds, Protein & Peptide Letters 2002; 9 (1) . https://dx.doi.org/10.2174/0929866023409002