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Bioorg Med Chem. 2004 Jun 1;12(11):2881-6.

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

Author information

1
Laboratório de Bioquímica do Instituto de Pesquisas em Patologias Tropicais, Porto Velho-RO, Brazil.

Abstract

The isolation and biochemical/enzymatic characterization of an L-amino acid oxidase, Balt-LAAO-I, from Bothrops alternatus snake venom, is described. Balt-LAAO-I is an acidic glycoprotein, pI approximately 5.37, homodimeric, Mr approximately 123,000, whose N-terminal sequence is ADVRNPLE EFRETDYEVL. It displays a high specificity toward hydrophobic and basic amino acids, while deglycosylation does not alter its enzymatic activity. Balt-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. Balt-LAAO-I is a multifunctional enzyme with promising relevant biotechnological and medical applications.

PMID:
15142548
DOI:
10.1016/j.bmc.2004.03.049
[Indexed for MEDLINE]

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