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Purification and partial characterization of a lectin from Caesalpinia tinctoria Domb, ex Dc fruits Braz. J. Plant Physiol.
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.
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...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Circular dichroism; Leguminosae; Plant defense; Pod; Secondary structure.
Ano: 2003 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1677-04202003000200008
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