Characterization Of A Hemagglutinating Glycoprotein Isolated From Bothrops Moojeni Snake Venom

Title: Characterization Of A Hemagglutinating Glycoprotein Isolated From Bothrops Moojeni Snake Venom

Volume: 8 Issue: 1

Author(s): B. H. Kassab, D. D. de Carvalho, S. Marangoni and J. C. Novello

Affiliation:

Keywords: HEMAGGLUTINATING, GLYCOPROTEIN, BOTHROPS MOOJENI, BmooL, carbohydrate recognition domain, Galectins, immunoglobulin-like, Mitogenic, T-lymphocytes, Cytotoxic

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.

Cite this article as:

Kassab H. B., de Carvalho D. D., Marangoni S. and Novello C. J., Characterization Of A Hemagglutinating Glycoprotein Isolated From Bothrops Moojeni Snake Venom, Protein & Peptide Letters 2001; 8 (1) . https://dx.doi.org/10.2174/0929866013409760