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BMC Proceedings

Open Access

Isolation and characterization of a lectin from Andira anthelmia seeds

  • Cleane Moreira1,
  • Mayara Silva1,
  • Camila Nobre2,
  • Thaiz Miguel1,
  • Antonia Nascimento1,
  • Celso Nagano1,
  • Kyria Nascimento1,
  • Benildo Cavada1 and
  • Ivanice Silva1
BMC Proceedings20148(Suppl 4):P238

Published: 1 October 2014


Fungicide ActionHemagglutinating ActivityRabbit ErythrocyteDivalent Metal CationVasorelaxant Effect

Andira anthelmia seeds, a species belonging to the Leguminosae family, Papilionoideae subfamily, Dalbergieae tribe, have a glucose/mannose specific lectin that agglutinates rabbit erythrocytes treated with trypsin. The Dalbergieae tribe has lectins which have specificity for different carbohydrates including mannose and also have several biological activities such as induction of rat paw edema, release of chemotactic mediators by macrophages, vasorelaxant effect in rat aortas, termiticide activity, potential fungicide action, among others. This study aimed to isolate, purify and physicochemically characterize a lectin found in seeds of Andira anthelmia. The lectin from Andira anthelmia seeds was purified by affinity chromatography on Mannose-Sepharose matrix followed by ion exchange chromatography on DEAE-Sephacel matrix. This procedure resulted in a purified lectin, named AAL. AAL purification process was monitored by specific hemagglutinating activity and SDS-PAGE, in which it was observed that this lectin has a molecular weight of approximately 20 kDa and four others subunits of approximately 15 and 14 kDa. This lectin is a glycoprotein with approximately 1.89% of carbohydrates on its composition and shows high stability, being able to maintain their hemagglutinating activity in a wide pH range and after exposure to temperatures of 70 °C for one hour. After dialysis against the chelating agent EDTA, AAL lost its hemagglutinating activity, but recovered its action after the addition of metals, being, therefore, dependent on divalent metal cations. In this study a new lectin from Dalbergieae was purified and characterized. Further analyzes are needed in order to best evaluate their biotechnological applications.

Authors’ Affiliations

Universidade Federal do Ceará, Fortaleza, Brazil
Universidade Regional do Cariri, Crato, Brazil


© Moreira et al.; licensee BioMed Central Ltd. 2014

This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The Creative Commons Public Domain Dedication waiver ( applies to the data made available in this article, unless otherwise stated.