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- Platelet aggregation and antibacterial effects of an L-amino acid oxidase purified from Bothrops alternatus snake venom
- Universidade Estadual Paulista (UNESP)
- Universidade Federal de São Carlos (UFSCar)
- 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.
- Bioorganic & Medicinal Chemistry. Oxford: Pergamon-Elsevier B.V., v. 12, n. 11, p. 2881-2886, 2004.
- Elsevier B.V.
- snake venom
- L-amino acid oxidase
- Bothrops alternatus
- bactericidal effect
- platelet aggregation
- biotechnological application
- Acesso restrito
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