Characterization of a lectin-like protein isolated from Lachesis muta snake venon

ABSTRACT

A lectin-like protein was isolated from L. muta venom by gel filtration on BIO Gel P-100 followed by column Chromatography on DEAE-Sephadex A-50. The protein eluted at 0.4 M NaCl in 0.01 Tris pH 7.3 and exhibited agglutinin activity toward 0**+ human erytrocytes. The protein is a dimer with Mr 28 kDa. Amino acid analysis revealed high content or tryptophan and acid recidues and low content of cysteine and methionine residues. No neural carbohydrates an sialic acid were detected. Circular dichroic spectrum shows 78% of B structure and 1% of alfa structure. In vitro experiments with ery throcytes from rat, rabbit and dog revealed strong agglutination while red blood cells from mice, sheep and goat were not agglutinated. In vivo experiments using non-anesthetized rats, a sharp and prolonged fall in the blood pressure was observed at protein dose of 1.5 mg/kg. Double dose of protein caused the death of the animal