Platelet aggregation and antibacterial effects of an L-amino acid oxidase purified from Bothrops alternatus snake venom

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Stabeli, R. G.
Marcussi, S.
Carlos, G. B.
Pietro, RCLR
Selistre-De-Araujo, H. S.
Giglio, JR
Oliveira, E. B.
Soares, A. M.

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Elsevier B.V.


The isolation and biochemical/enzymatic characterization of an L-amino acid oxidase, Balt-LAAO-I, from Bothrops alternates snake venom, is described. Balt-LAAO-I is an acidic glycoprotein, pI similar to 5.37, homodimeric, M-r similar to 123, 000, whose Nterminal sequence is ADVRNPLE EFRETDYEVL. It displays a high specificity toward hydrophobic and basic amino acids, while deglycosylation does not alter its enzymatic activity. Bait-LAAO-I induces platelet aggregation and shows bactericidal activity against Escherichia coli and Staphylococcus aureus. In addition, this enzyme is slightly hemorrhagic and induces edema in the mouse paw. Bait-LAAO-I is a multifunctional enzyme with promising relevant biotechnological and medical applications. (C) 2004 Elsevier Ltd. All rights reserved.



snake venom, L-amino acid oxidase, Bothrops alternatus, bactericidal effect, platelet aggregation, biotechnological application

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Bioorganic & Medicinal Chemistry. Oxford: Pergamon-Elsevier B.V., v. 12, n. 11, p. 2881-2886, 2004.