Use of cholesterol-loaded cyclodextrin: An alternative for bad cooler stallions

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Chromosomal Mapping of Repetitive DNA and Cytochrome C Oxidase I Sequence Analysis Reveal Differentiation among Sympatric Samples of Astyanax fasciatus (Characiformes, Characidae)

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Molecular characterization of fire ants, Solenopsis spp., from Brazil based on analysis of mtDNA gene cytochrome oxidase I

Species from the Solenopsis saevissima (Smith) (Hymenoptera: Formicidae) species group are native to South America and have a cosmopolitan distribution because they have been accidentally introduced in many countries around the world. In Brazil, they have a wide distribution, including urban areas. The present study was conducted to investigate the characterization of Solenopsis genus populations associated with urban/human interference sites in Brazil by analyzing the mitochondrial gene cytochrome oxidase I and estimating the degree of relatedness of these populations to make inferences about their phylogeny and also observe the patterns of mitochondrial haplotype (mitotype) distribution across their range. The results revealed complete geographical coherence and polyphyly for the Solenopsis invicta Buren and Solenopsis saevissima species groups, which confirms the diversity of the genera. It also suggests the possibility that reproductively-isolated populations occur, resulting in the evolutionary process of speciation. No predominant haplotype was found in the populations analyzed, but some were more prevalent.

The negligible effects of the antifungal natamycin on cholesterol-dipalmitoyl phosphatidylcholine monolayers may explain its low oral and topical toxicity for mammals

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Crystallization and preliminary X-ray diffraction studies of an L-amino-acid oxidase from Lachesis muta venom

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Produção de enzimas ligninolíticas, glioxal oxidase e proteases por fungos marinhos

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Síntese e estudo da diapocinina como um inibidor da NADPH Oxidase em neutrófilos e células mononucleares de sangue periférico

Apocynin, a methoxy-catechol originally extracted from the root of Picrorhiza kurroa, has been used as an inhibitor of the NADPH oxidase complex in phagocytic and nonphagocytic cells. Its mechanism of inhibition is linked to their prior activation through the action of peroxidases leading to oxidation of the dimeric product, diapocynin. In this study, dipocinina was synthesized and investigated its effect as an inhibitor of activation NADPH oxidase in neutrophils (PMN) and peripheral blood mononuclear cells (PBMC). The synthesis of diapocinina was performed by oxidation of apocinina by potassium persulphate in the midst of water for 5 minutes at room temperature. The precipitate was filtered and washed with water and methanol. Diapocinina was characterized by mass spectrometry. PMN and PBMC were obtained from peripheral blood of healthy donors and purified for gelatin sedimentation, or centrifugation with Histopaque ®, the red cells were lysed with ice water or ammonium chloride. Diapocinina or apocinina were incubated with opsonized zymosan, activation of PMNs and release of superoxide anion, these monitored by chemiluminescent assay dependent lucigenina. We found that diapocinina inhibitor was no better than the apocinina in PMN. However, diapocinina was more efficient than apocinina as an inhibitor of NADPH oxidase in PBMC. In conclusion, whereas PBMC are relatively poor compared with peroxidases PMN, our results are consistent with the need for oxidation apocinina for its effect as an inhibitor of NADPH oxidase

Análise das sequências do gene mitocondrial citocromo C oxidase e caracterização de ninhos de Trachymyrmex tucumanus Forel, 1914 (Hymenoptera, Formicidae)

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Supplementation with sunflower seed increases circulating cholesterol concentrations and potentially impacts on the pregnancy rates in Bos indicus beef cattle

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Polyphenol oxidase from sweet potato: Purification and properties

Polyphenol oxidase (PPO, EC 1.14.18.1) extracted from sweet potato root [Ipomoea batatas (L.) Lam.] was purified 189-fold by precipitation with ammonium sulfate and elution from columns of Sephadex G-25, DEAE-cellulose, and Sephadex G-100. Polyacrylamide gel electrophoresis of the purified preparation revealed that PPO was highly purified by the procedure adopted. The purified enzyme had an estimated molecular weight of 96 000 and Km values of 26, 8, 5, and 96 mM for 4-methylcatechol, chlorogenic acid, caffeic acid, and catechol, respectively. The optimum pH varies from about 4.0 to 6.5, depending on the substrate. PPO activity was inhibited by p-coumaric and cinnamic acids, sodium metabisulfite, dithioerythritol, ascorbic acid, L-lysine, D-phenylalanine, L-methionine, glycine, L-isoleucine, and L-glutamine. Heat inactivation between 60 and 80 °C was biphasic. Sucrose, (NH4)2SO4, NaCl, and KCl appeared to be protective agents of sweet potato PPO against thermal denaturation. © 1992 American Chemical Society.

Artifactual oxidation of cholesterol during the analysis of cholesterol oxidation products: protective effect of antioxidants

To study the influence of the addition of various antioxidants and their combinations on the artifactual oxidation of cholesterol during analysis, 2 factorial experiments were performed in duplicate. In the first experiment, 2 amounts of the following antioxidants were assayed: ethylenediaminetetraacetic acid (EDTA) disodium salt (0 and 1 mg), pyrogallol (0 and 600 microg), and butylated hydroxytoluene (BHT; 0 and 600 microg); in the second, EDTA disodium salt (0 and 1 mg), ascorbyl palmitate (0 and 600 microg), and BHT (0 and 600 microg). Under low oxidative conditions of dim light, evaporation of solvents at low temperatures, and cold saponification in darkness under nitrogen atmosphere, the addition of antioxidants showed no further protective effect. Furthermore, the presence of ascorbyl palmitate significantly increased the formation of cholesterol-5beta,6beta-epoxide, and 7beta-hydroxycholesterol.

The importance of myeloperoxidase in apocynin-mediated NADPH oxidase inhibition

Apocynin is widely used as an inhibitor of the NADPH oxidase. Since myeloperoxidase (MPO) has been considered as essential for the mechanism of action of apocynin, here we used cells with different levels of MPO and compared their sensitivity to apocynin. HL-60 cells were differentiated with DMSO or IFN γ /TNF α and compared with peripheral mononuclear (PBMC) and polymorphonuclear cells (PMN). The relative MPO activity was PBMC = HL60 DMSO < HL60 IFN γ < PMN. Apocynin inhibited the intracellular reactive oxygen species production by PMN (80%) and IFN γ /TNF α -differentiated HL-60 cells (45%) but showed a minor effect in PBMC and DMSO differentiated HL-60 cells (20%). The addition of azide decreased the efficiency of apocynin in PMN and the addition of peroxidase increased the inhibition in PBMC. We also determined the gene expression of the components gp91phox, p47phox, p22phox and p67phox in the resting cells. Apocynin did not change gp91phox, p47phox or p22phox gene expression in nonstimulated PBMC, HL60 DMSO, HL60 IFN γ /TNF α , and PMN and has a subtle increase in p67phox in HL60 IFN γ /TNF α . The results from this work suggest that a rational search for better inhibitors of NADPH oxidase in leukocytes should include a correlation with their affinity as substrates for MPO.