L Amino Acid Oxidases
Mostrando 1-12 de 20 artigos, teses e dissertações.
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1. BjussuLAAO-II induces cytotoxicity and alters DNA methylation of cell-cycle genes in monocultured/co-cultured HepG2 cells
Abstract Background: The use of animal venoms and their toxins as material sources for biotechnological applications has received much attention from the pharmaceutical industry. L-amino acid oxidases from snake venoms (SV-LAAOs) have demonstrated innumerous biological effects and pharmacological potential against different cancer types. Hepatocellular carc
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 11/03/2019
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2. Kinetic investigations and stability studies of two Bothrops L-amino acid oxidases
Abstract Background: L-amino acid oxidases isolated from snake venoms (SV-LAAOs) are enzymes that have great therapeutic potential and are currently being investigated as tools for developing new strategies to treat various diseases, including cancer and bacterial infections. The main objective of this study was to make a brief evaluation of the enzymatic s
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 24/01/2019
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3. Bordonein-L, a new L-amino acid oxidase from Crotalus durissus terrificus snake venom: isolation, preliminary characterization and enzyme stability
BackgroundCrotalus durissus terrificus venom (CdtV) is one of the most studied snake venoms in Brazil. Despite presenting several well known proteins, its L-amino acid oxidase (LAAO) has not been studied previously. This study aimed to isolate, characterize and evaluate the enzyme stability of bordonein-L, an LAAO from CdtV.Methods The enzyme was isolated th
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 29/09/2015
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4. Snake venom L-amino acid oxidases: an overview on their antitumor effects
The L-amino acid oxidases (LAAOs) constitute a major component of snake venoms and have been widely studied due to their widespread presence and various effects, such as apoptosis induction, cytotoxicity, induction and/or inhibition of platelet aggregation, hemorrhage, hemolysis, edema, as well as antimicrobial, antiparasitic and anti-HIV activities. The iso
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 11/07/2014
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5. Cloning, characterization and expression of a novel laccase gene Pclac2 from Phytophthora capsici
Laccases are blue copper oxidases (E.C. 1.10.3.2) that catalyze the one-electron oxidation of phenolics, aromatic amines, and other electron-rich substrates with the concomitant reduction of O2 to H2O. A novel laccase gene pclac2 and its corresponding full-length cDNA were cloned and characterized from Phytophthora capsici for the first time. The 1683 bp ful
Braz. J. Microbiol.. Publicado em: 08/04/2014
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6. AÃÃo antibacteriana antifÃngica e antiparasitÃria de veneno de serpentes do gÃnero Bothrops e suas fraÃÃes fosfolipase A2 e L-AminoÃcido oxidase / Antibacterial, antifungal and antiparasitary action of Bothrops venoms and their fractions phospholipase A2 and L-aminoacid oxidase
Snakes venoms contain biologically active substances primarily consisting of proteins (90-95%). Some of these present enzymatic activities, such as phospholipases A2 and the L-amino acid oxidases. In this study we verify the action of Bothrops leucurus (BleuTV) and Bothrops marajoensis (BmarTV) venoms, and fractions PLA2 (BleuPLA2 and BmarPLA2) and LAAO (Ble
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 08/04/2009
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7. Structural and functional caracterization of L-aminoácido oxidases isolated from snake Bothrops venoms / Caracterização funcional e estrutural de L-aminoácido oxidases isoladas de venenos de serpentes do gênero Bothrops
The aim of this project was the isolation of three L-aminoacid oxidases from Bothrops jararaca, Bothrops moojeni and Bothrops pirajai snake venoms, respectively, in addition to their biochemical, enzymatic, pharmacological and toxicological characterization. They were named BjarLAAO-I, BmooLAAO-I and BpirLAAO-I, respectively, and their isolation involved two
Publicado em: 2008
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8. Effects of Bothrops insularis venom and its isolated fractions on renal and vascular systems / Avaliação dos efeitos renais e vasculares do veneno da Bothrops insularis e de frações isoladas
Foram investigados os efeitos do veneno da serpente Bothrops insularis e de suas frações, lectina, L-aminoácido oxidase, trombina símile e fosfolipase A2, no rim isolado e sistema vascular de rato. As frações foram purificadas a partir de uma combinação de procedimentos cromatográficos, usando colunas de HPLC de exclusão molecular, troca iônica, f
Publicado em: 2006
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9. Demonstration of Imino Acids as Products of the Reactions Catalyzed by D- and L-Amino Acid Oxidases
It had long been thought, but never demonstrated, that imino acids are formed in the reactions catalyzed by D- and L-amino acid oxidases (EC 1.4.3.3 and 1.4.3.2). The formation of imino acids is now shown directly by allowing the amino acid oxidase reaction to proceed in the presence of NaBH4, when the imino acid is reduced to the corresponding racemic amino
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10. Amino acid oxidase of leukocytes in relation to H2O2-mediated bacterial killing
D-Amino acid oxidase and L-amino acid oxidase have been measured in sucrose homogenates of polymorphonuclear leukocytes (PMN) obtained from guinea pigs and humans. Subcellular distribution patterns and studies on latency indicate that these oxidases are soluble enzymes. Their hydrogen peroxide-generating capacity was verified. Chronic granulomatous disease P
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11. PROLINE OXIDASES IN HANSENULA SUBPELLICULOSA
Ling, Chung-Mei (Illinois Institute of Technology, Chicago), and L. R. Hedrick. Proline oxidases in Hansenula subpelliculosa. J. Bacteriol. 87:1462–1470. 1964—Cells of Hansenula subpelliculosa can use l-proline as a carbon and a nitrogen source after a 6- to 8-hr induction period. However, they cannot use l-glutamate as both nitrogen and carbon sources u
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12. l-amino acid oxidases of Proteus rettgeri.
Proteus rettgeri has been found to contain two separable 1-amino acid oxidases. Both enzymes are particulate in nature, neither being ribosomal bound. One of these enzymes appears to have broad specificity, being active toward monoaminomonocarboxylic, imino, aromatic, sulfur-containing, and beta-hydroxyamino acids. The other enzyme has more limited specifici