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.

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

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866023409002

Publication date: 2002-02-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.