Characterization Of A Hemagglutinating Glycoprotein Isolated From Bothrops Moojeni Snake Venom

Authors: Kassab B.H.; de Carvalho D.D.; Marangoni S.; Novello J.C.

Source: Protein and Peptide Letters, Volume 8, Number 1, February 2001 , pp. 13-20(8)

Publisher: Bentham Science Publishers

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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; Mitogenic; T-lymphocytes; Cytotoxic