Data/hora: 11/06/2024 02:25:13

Provedor de dados: 	61	
País: 	Brazil	
Título: 	Purification and partial characterization of a lectin from Caesalpinia tinctoria Domb, ex Dc fruits	
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.	
Data: 	2003-08-01	
Ano: 	2003	
Palavras-chave: 	Circular dichroism; Leguminosae; Plant defense; Pod; Secondary structure.	
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).	
Tipo: 	Info:eu-repo/semantics/article	
Idioma: 	Inglês	
Identificador: 	http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1677-04202003000200008	
Editor: 	Brazilian Journal of Plant Physiology	
Relação: 	10.1590/S1677-04202003000200008	
Formato: 	text/html	
Fonte: 	Brazilian Journal of Plant Physiology  v.15 n.2 2003	
Fonte: 	info:eu-repo/semantics/openAccess