Inhibition of the myotoxic activity of Bothrops asper myotoxin II in mice by immunization with its synthetic 13-mer peptide 115–129

Author:

Calderón Leonel,Lomonte Bruno

Publisher

Elsevier BV

Subject

Toxicology

Reference14 articles.

1. Structure of a calcium-independent phospholipase-like myotoxic protein from Bothrops asper venom;Arni;Acta Cryst. D,1995

2. Calderón, L., Lomonte, B., 1998. Immunochemical characterization and role in toxic activities of region 115--129 of myotoxin II, a Lys49 phospholipase A2 from Bothrops asper snake venom. Arch. Biochem. Biophys. 358 (in press)

3. Cleavage of the NH2-terminal octapeptide of Bothrops asper myotoxic lysine-49 phospholipase A2 reduces its membrane-destabilizing effect;Dı́az;Arch. Biochem. Biophys.,1994

4. Fletcher, J.E., Selistre de Araujo, H.S., Ownby, C.L., 1997. Molecular events in the myotoxic action of phospholipases. In: Kini, R.M. (Ed.), Venom Phospholipase A2 Enzymes: Structure, Function, and Mechanism. John Wiley and Sons, England, pp. 455–497

5. Myotoxin II from Bothrops asper (terciopelo) venom is a lysine-49 phospholipase A2;Francis;Arch. Biochem. Biophys.,1991

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