| Autor: |
Ceccatto VM; Depto de Geociências/Universidade Estadual do Ceará, Caixa Postal 6033, CEP 60451-970, Fortaleza-Ceará, Brasil., Cavada BS, Nunes EP, Nogueira NA, Grangeiro MB, Moreno FB, Teixeira EH, Sampaio AH, Alves MA, Ramos MV, Calvete JJ, Grangeiro TB |
| Jazyk: |
angličtina |
| Zdroj: |
Protein and peptide letters [Protein Pept Lett] 2002 Feb; Vol. 9 (1), pp. 67-73. |
| DOI: |
10.2174/0929866023409002 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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