Artículos de revistas
Characterization of a hemagglutinating glycoprotein isolated from Bothrops moojeni snake venom
Registro en:
Protein And Peptide Letters. Bentham Science Publ Ltd, v. 8, n. 1, n. 13, n. 20, 2001.
0929-8665
WOS:000166906400002
10.2174/0929866013409760
Autor
Kassab, BH
de Carvalho, DD
Marangoni, S
Novello, JC
Institución
Resumen
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. 8 1 13 20