| Registro completo |
| Provedor de dados: |
Braz. J. Plant Physiol.
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| País: |
Brazil
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| Título: |
Purification and partial characterization of a lectin from Caesalpinia tinctoria Domb, ex Dc fruits
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| Autores: |
Oliveira,Marli Lourdes de
Beltramini,Leila Maria
Simone,Salvatore Giovanni de
Brumano,Maria Helena Nasser
Silva-Lucca,Rosemeire Aparecida
Nakaema,Marcelo Kiyoshi Kian
Pires,Christiano Vieira
Oliveira,Maria Goreti de Almeida
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| Data: |
2003-08-01
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| Ano: |
2003
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| Palavras-chave: |
Circular dichroism
Leguminosae
Plant defense
Pod
Secondary structure
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| Resumo: |
A lectin was isolated from the pod saline extract of Caesalpinia tinctoria by dialoconcentration on Centripep-10 and affinity chromatography on chitin column. The purified lectin was partially characterized with respect to its biochemical and structural properties. It contains 8.3 % of carbohydrate and exhibited an agglutinating activity against human erythrocytes (ABO groups). Its amino acid composition was characterized by a great number of acidic and hydrophobic residues and the estimated molecular mass was 12.5 kDa. The presence of only one N-terminal amino acid sequence (D¹-V-P-A-Y-V-Y-V-H-F10-G-F-G-E-E-H-R -D-V-F20-D), showed the homogeneity of the purified lectin. The far-ultraviolet circular dichroism (CD) spectrum of lectin indicated that it contains 10 % a-helix, 38 % b-sheet, 28 % unordered form and 6 % of P II (poly-L-proline II helix conformation).
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| Tipo: |
Info:eu-repo/semantics/article
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| Idioma: |
Inglês
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| Identificador: |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1677-04202003000200008
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| Editor: |
Brazilian Journal of Plant Physiology
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| Relação: |
10.1590/S1677-04202003000200008
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| Formato: |
text/html
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| Fonte: |
Brazilian Journal of Plant Physiology v.15 n.2 2003
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| Direitos: |
info:eu-repo/semantics/openAccess
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