Lectins are ubiquitous (glyco)proteins, which exhibit specific and reversible carbohydrate-binding activities. These proteins combine, reversible and non-covalently, with mono or oligosaccharides free in solution or attached to cell surface. Their large application on biotechnological and medical field made these proteins target to several studies. In the Laboratório de Química de Proteínas several plants have been screened as lectins source, and one of the most promising was Brosimum gaudichaudii (mama-cadela).  In this work the lectin of mama-cadela was partially purified, characterized, immobilized in poly(aniline).  Crude extracts were made with 0.15 mol L^-1 saline solution and 0.1 mol L^-1 glycine buffer, pH 2.6 and 9.0. The amount of protein extracted with saline solution was 12,3 mg g^-1 and a specific activity of 5392,5 HU mg^-1 of protein. The hemagglutination assay showed the lectin was Ca ²⁺ and Mn ²⁺ non-dependent. The crude extract was heated to determine thermal stability of the lectin. This test showed the hemagglutinating activity was abolished after heating at 90ºC for 30 min. The tests of sugar inhibition showed that mama-cadela lectin have high affinity for lactose and galactose. The lectin was able to hemagglutinating positive for rabbit blood and all human blood groups (A, B, AB and O). The purification was carried out by ammonium sulfate precipitation (up to 80%), followed by gel filtration in a Sephadex G-75 column (42 / 2 cm).  This proceeding resulted in a partial purification as reveleded the SDS-PAGE electrophoresis. The lectin (crude extract) was submitted to immobilization in polianiline activated with glutaraldehyde, in a proportion of 1.0 ml to 5.0 or 10.0 mg of support. The immobilized lectin was able to remove 30% of lactose present in a test solution. This preliminary tests showed that mama-cadela lectin is a potential protein for exploitation in the fields of alimentary and affinity chromatography for glycoconjugates isolation.