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Isolation, purification and partial physicochemical characterization of a lectin in Andira pisonis Mart seed

  • Claudia Figueiredo Lossio1,
  • Mayara Torquato Lima da Silva1,
  • Lia Monteiro Barbosa1,
  • Cleane Gomes Moreira1,
  • Thaiz Batista Azevedo Rangel Miguel1,
  • Antonia Samia Fernandes do Nascimento1,
  • Ivanice Bezerra da Silva1,
  • Kyria Santiago do Nascimento1 and
  • Benildo Sousa Cavada1
BMC Proceedings20148(Suppl 4):P226

Published: 1 October 2014


MannoseSodium AcetateTotal Protein ExtractionHemagglutination ActivityBiotechnological Potential

Lectins are ubiquitous proteins in nature, with non-immune origin, which have at least one non-catalytic domain that binds carbohydrates specifically and reversibly. They can be found in vegetables leaves, stems and seeds. The Dalbergieae tribe has lectins which have specificity for different carbohydrates and also have several biological activities such as induction of rat paw edema, release of chemotactic mediators by macrophages, vasorelaxant effect in rat aortas, among others. This study aimed to isolate, purify and physiochemically characterize a lectin found in seeds of Andira pisonis Mart (Dalbergieae). Andira pisonis Mart seeds were ground into a fine powder and subjected to total protein extraction in 1 M ammonium sulfate. Soluble proteins were subjected to hemagglutination activity quantification by the Bradford method and essays of hemagglutination inibition activity by sugar. The lectin from Andira pisonis Mart (APL) was purified by affinity chromatography on Sepharose- Mannose matrix eluted in 0.1 M glycine buffer pH 2.6 with 0.15 M NaCl. The eluted fraction was dialyzed against distilled water, lyophilized and subjected to ion exchange chromatography on HiTrap SP XL 01. APL was eluted on 20 mM sodium acetate buffer pH 4.5 gradient of 0-1M NaCl. APL hemagglutinated rabbit erythrocytes (enzymatically treated) and other lectins from the tribe Dalbergieae and showed specificity for mannose (25 mM). SDS-PAGE analysis showed that APL is composed of a major 34 kDa double band and a minor 8 and 9 kDa double band. APL showed thermostability at 60° C. Further studies are still needed in order to better physicochemically characterize this protein and study its biotechnological potential on the referred conditions of vasorelaxant effect and chemotatic mediator.

Authors’ Affiliations

Universidade Federal do Ceara, Fortaleza, Brazil


© Lossio 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.