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

Authors: Ceccatto V.M.; Cavada B.S.; Nunes E.P.; Nogueira N.A.P.; Grangeiro M.B.; Moreno F.B.M.B.; Teixeira E.H.; Sampaio A.H.; Alves M.A.O.; Ramos M.V.; Calvete J.J.; Grangeiro T.B.

Source: Protein and Peptide Letters, Volume 9, Number 1, February 2002 , pp. 67-73(7)

Publisher: Bentham Science Publishers

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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 ( agr chain), 16-18 kDa ( bgr fragment) and 12-13 kDa ( ggr 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.