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Characterization Of A Hemagglutinating Glycoprotein Isolated From Bothrops Moojeni Snake Venom

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

Document Type: Review Article


Publication date: February 1, 2001

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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