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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Characterization Of A Hemagglutinating Glycoprotein Isolated From Bothrops Moojeni Snake Venom

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

Volume 8, Issue 1, 2001

Page: [13 - 20] Pages: 8

DOI: 10.2174/0929866013409760


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

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