Purification and partial characterization of a lectin from Canavalia grandiflora benth. seeds

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 (alpha chain), 16-18 kDa (beta fragment) and 12-13 kDa (gamma fragment...

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Bibliographic Details
Published inProtein and peptide letters Vol. 9; no. 1; p. 67
Main 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
Format Journal Article
LanguageEnglish
Published Netherlands 01.02.2002
Subjects
Amino Acids - metabolism
Animals
Chromatography, Affinity
Electrophoresis, Polyacrylamide Gel
Erythrocytes - metabolism
Fabaceae - chemistry
Fabaceae - genetics
Fabaceae - metabolism
Haptens - metabolism
Hemagglutination
Humans
Lectins - chemistry
Lectins - isolation & purification
Lectins - metabolism
Plant Lectins
Rabbits
Seeds - chemistry
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Summary: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 (alpha chain), 16-18 kDa (beta fragment) and 12-13 kDa (gamma 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.
ISSN:0929-8665
1875-5305
DOI:10.2174/0929866023409002