Abstract
From the crude snake venom of Bothrops moojeni, a homodimeric lectin was purified by affinity chromatography in lactose and was named BMooL. This lectin appeared to be a glycoprotein because it reacted with Schiffs reagent. The hemagglutinating activity of BMooL is inhibited by galactoside, EDTA, EGTA and DTT. The amino acid analysis of BMooL showed a high content of acidic residues and its N-terminal sequence showed similarity with other lectins from snake venoms.
Keywords: HEMAGGLUTINATING, GLYCOPROTEIN, BOTHROPS MOOJENI, BmooL, carbohydrate recognition domain, Galectins, immunoglobulin-like, Mitogenic, T-lymphocytes, Cytotoxic