Purification and partial characterization of a lectin from Caesalpinia tinctoria Domb, ex Dc fruits

Abstract

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).

Insights into Animal and Plant Lectins with Antimicrobial Activities

“…Furthermore, other lectins have already been elucidated, such as ricin, a lectin from Ricinus communis , which exhibited a combination of α-helices and β-sheets [2]. Oliveira and coworkers [133] also demonstrated a similar scaffold for a lectin purified from Caesalpinia tinctoria [133]. In most, the tertiary structure conformation of lectins presents structurally dominant β-sheets combined with the presence of α-helices that can also be absent.…”

Estudios Estructura Y Función De Una Lectina Aislada De Semillas De Caesalpinia Spinosa Kuntze (Tara)

“…En el presente estudio se ha encontrado que la lectina de Caesalpinia spinosa (CsLEC) purificada a partir de semillas corresponde a una proteína con un alto porcentaje de aminoácidos hidrofóbicos, lo que al parecer indicaría que se trata de una proteína altamente compacta y estable, y con un peso molecular de alrededor de 29 KDa. Oliveira et al (2003) encontraron que la lectina purificada a partir del fruto (vaina) de la tara presentó un alto número de residuos ácidos e hidrofóbicos, y su peso molecular fue de ~12,5 kDa. En ambas lectinas purificadas de tara (semilla y fruto) existe un alto contenido de aminoácidos hidrofóbicos, pero el peso molecular fue mayor en la semilla (~ 29,19 kDa) que en la vaina.…”