Isolation and characterization of a new lectin from the venom of the snake Bothrops jararacussu

Abstract

Bothrops jararacussu venom contains a new potent hemagglutinin (BJcuL), isolated by affinity chromatography on immobilized D-galactose. Hemagglutination activity of BJcuL against pig erythrocytes was inhibited by galactosides, EDTA or EGTA. The purified lectin is a di sulfide dimer composed of 15 kDa subunits. Association of these subunits is essential for lectin activity, since DTT-reduced BJcuL showed no hemagglutination activity against pig erythrocytes. Reduced and S-pyridylethylated BJcuL (RP-BJcuL) was separated as a single peak by reverse-phase HPLC on a C-18/μBondapak column. Results of the application of Edman degradation methodology showed that RP-BJcuL has a single N-terminal amino acid sequence, indicating that BJcuL is a homodimer. The N-terminal 8-residue (NNCPQDWL) shows homology with other lectins from snake venoms.