Purification and biological effects of l-amino acid oxidase isolated from Bothrops insularis venom

Braga, Marcus Davis Machado; Martins, Alice Maria Costa; Amora, Daniela Nascimento; Menezes, Dalgimar Beserra de; Toyama, Marcos Hikari; Toyama, Daniela O.; Marangoni, Sérgio; Alves, Claudênio Diógenes; Barbosa, Paula; Alves, Renata de Sousa; Fonteles, M. C.; Monteiro, Helena Serra Azul

doi:10.1016/j.toxicon.2007.09.003

Cited by 36 publications

(23 citation statements)

References 28 publications

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“…The liberated H 2 O 2 has various effects on cell metabolism such as inducing apoptosis, as well as bactericidal and bacteriostatic effects [7,32]. Although the detailed mode of antibacterial action of H 2 O 2 is not fully understood, H 2 O 2 could induce oxidative stress to the targeted cells, initiate cell membrane and cytoplamatic disorganization and consequently causes the cells death [33,34].…”

Section: Discussionmentioning

confidence: 99%

The serum of rabbitfish (Siganus oramin) has antimicrobial activity to some pathogenic organisms and a novel serum l-amino acid oxidase is isolated

Wang

Xie

et al. 2011

Fish & Shellfish Immunology

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Section: Discussionmentioning

confidence: 99%

The serum of rabbitfish (Siganus oramin) has antimicrobial activity to some pathogenic organisms and a novel serum l-amino acid oxidase is isolated

Wang

Xie

et al. 2011

Fish & Shellfish Immunology

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“…The byproduct, hydrogen peroxide, is thought to be responsible for its toxic effects. This group of enzymes is one of the most common components of snake venoms [116][117][118][119][120][121][122][123][124][125] and is responsible for the yellow color of the venom. Structurally, they are homodimers with a molecular weight of 110-150 kDa.…”

Section: Snake Venom L-amino Acid Oxidase (Sv-laaos)mentioning

confidence: 99%

Protein complexes in snake venom

Doley

Kini

2009

Cell. Mol. Life Sci.

202

125

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Snake venom contains mixture of bioactive proteins and polypeptides. Most of these proteins and polypeptides exist as monomers, but some of them form complexes in the venom. These complexes exhibit much higher levels of pharmacological activity compared to individual components and play an important role in pathophysiological effects during envenomation. They are formed through covalent and/or non-covalent interactions. The subunits of the complexes are either identical (homodimers) or dissimilar (heterodimers; in some cases subunits belong to different families of proteins). The formation of complexes, at times, eliminates the non-specific binding and enhances the binding to the target molecule. On several occasions, it also leads to recognition of new targets as protein-protein interaction in complexes exposes the critical amino acid residues buried in the monomers. Here, we describe the structure and function of various protein complexes of snake venoms and their role in snake venom toxicity.

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“…Some purified Bothrops toxins are able to reproduce the renal effects obtained with whole venom. Studies on the isolated perfused rat kidney have shown that L-amino acid oxidase (Braga et al, 2008), C-type lectins (Braga et al, 2006), phospholipase A2 myotoxins (Barbosa et al, 2005;Evangelista et al, 2010) and thrombin-like enzyme (Braga et al, 2007) from Bothrops venoms can alter renal function. The isolated perfused kidney technique also confirmed the direct acute tubular nephrotoxicity of Bothrops venoms and showed that platelet activating factor might play a role in some renal functional disturbances such as the decreased in glomerular filtration rate (Monteiro and Fonteles, 1999).…”

Section: Bothrops Venommentioning

confidence: 99%