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| Registros recuperados: 131 | |
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| Rao,M.A; Scelza,R; Scotti,R; Gianfreda,L. |
| Environmental pollution is growing more and more due to the indiscriminate and frequently deliberate release of hazardous, harmful substances. Research efforts have been devoted to develop new, low-cost, low-technology, eco-friendly treatments capable of reducing and even eliminating pollution in the atmosphere, the hydrosphere and soil environments. Among biological agents, enzymes have a great potentiality to effectively transform and detoxify polluting substances because they have been recognized to be able to transform pollutants at a detectable rate and are potentially suitable to restore polluted environments. This brief review will examine some classes of pollutants and enzymes capable of transforming them effectively into innocuous products.... |
| Tipo: Journal article |
Palavras-chave: Pollutants; Enzymes; Environmental pollution; Bioremediation. |
| Ano: 2010 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0718-95162010000100008 |
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| Tan,NH; Fung,SY; Ponnudurai,G. |
| Bungarus flaviceps (red-headed krait) venom presents an intravenous LD50 of 0.32 μg/g and exhibits enzymatic activities similar to other Bungarus toxins. ELISA cross-reactions between anti-Bungarus flaviceps and a variety of elapid and viperid venoms were observed in the current study. Double-sandwich ELISA was highly specific, since anti-B. flaviceps serum did not cross-react with any tested venom, indicating that this assay can be used for species diagnosis in B. flaviceps bites. In the indirect ELISA, anti-B. flaviceps serum cross-reacted moderately with three different Bungarus venoms (9-18%) and Notechis scutatus venom, but minimally with other elapid and viperid toxins. The results indicated that B. flaviceps venom shares common epitopes with other... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Bungarus flaviceps venom; Enzymes; ELISA; Neutralization. |
| Ano: 2010 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992010000100014 |
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| Severo Gomes,B; Souza Motta,CM; Lima,AN; Porto,ALF. |
| In order to evaluate the pathogenicity of yeasts isolated from vaginal secretion of pregnant and non-pregnant women - stored in mineral oil at the URM Mycology Collection, Department of Mycology, Federal University of Pernambuco - 30 samples belonging to the genera Candida, Rhodotorula, Trichosporon, and Kloeckera, were studied regarding their pathogenic characteristics, ability to grow at room temperature (28°C ± 1°C), 37°C, and 42°C for 72 hours, and production of both phospholipase and proteinase. Results showed that all 30 isolates (100%) were able to grow at room temperature and 37°C, and that 17 samples (57%) were able to grow at 42°C. Evaluation of enzymatic activity showed protease activity in only two isolates (7%), namely C. maritima and C.... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Pathogenicity; Yeasts; Enzymes. |
| Ano: 2011 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000400013 |
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| Amorim,Fernanda Gobbi; Longhim,Heloisa Tavoni; Cologna,Camila Takeno; Degueldre,Michel; Pauw,Edwin De; Quinton,Loïc; Arantes,Eliane Candiani. |
| Abstract Background: Tityus serrulatus venom (Ts venom) is a complex mixture of several compounds with biotechnological and therapeutical potentials, which highlights the importance of the identification and characterization of these components. Although a considerable number of studies have been dedicated to the characterization of this complex cocktail, there is still a limitation of knowledge concerning its venom composition. Most of Ts venom studies aim to isolate and characterize their neurotoxins, which are small, basic proteins and are eluted with high buffer concentrations on cation exchange chromatography. The first and largest fraction from carboxymethyl cellulose-52 (CMC-52) chromatography of Ts venom, named fraction I (Fr I), is a mixture of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Tityus serrulatus; Scorpion venom; Enzymes; Proteases; ACE inhibitors; Proteome. |
| Ano: 2019 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992019000100308 |
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| Tan,CH; Sim,SM; Gnanathasan,CA; Fung,SY; Ponnudurai,G; Pailoor,J; Tan,NH. |
| Hypnale hypnale (hump-nosed pit viper) has been recently identified as one of the medically important venomous snakes in Sri Lanka and on the southwestern coast of India. The characterization of its venom is essential for understanding the pathophysiology of envenomation and for optimizing its management. In the present study, the biological properties of Hypnale hypnale venom and venom fractions obtained using Resource Q ion exchange chromatography were determined. The venom exhibited toxic activities typical of pit viper venom, comparable to that of its sister taxon, the Malayan pit viper (Calloselasma rhodostoma). Particularly noteworthy were its high activities of thrombin-like enzyme, proteases, phospholipase A2, L-amino acid oxidase and... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Hypnale hypnale; Venom; Enzymes; Toxins; Fibrinogen; Nephrotoxicity. |
| Ano: 2011 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000400015 |
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| Lima,P. R. de; Brochetto-Braga,M. R.. |
| Hymenoptera venoms are complex mixtures containing simple organic molecules, proteins, peptides, and other bioactive elements. Several of these components have been isolated and characterized, and their primary structures determined by biochemical techniques. These compounds are responsible for many toxic or allergic reactions in different organisms, such as local pain, inflammation, itching, irritation, and moderate or severe allergic reactions. The most extensively characterized Hymenoptera venoms are bee venoms, mainly from the Apis genus and also from social wasps and ant species. However, there is little information about other Hymenoptera groups. The Apis venom presents high molecular weight molecules - enzymes with a molecular weight higher than... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Hymenoptera; Venom; Enzymes; Peptides. |
| Ano: 2003 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992003000200002 |
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| Registros recuperados: 131 | |
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