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4.
Mem. Inst. Oswaldo Cruz ; 104(7): 1035-1038, Nov. 2009. ilus, tab
Artigo em Inglês | LILACS | ID: lil-534172

RESUMO

The molluscicidal activity of Hammada scoparia leaf extracts and the principal alkaloids isolated from them (carnegine and N-methylisosalsoline) were tested against the mollusc gastropod, Galba truncatula, the intermediate host of Fasciola hepatica in Tunisia. The results indicated that the molluscicidal activity was correlated with the presence of alkaloids. A significant molluscicidal value, according to the World Health Organization, was found with the methanol extract (LC50 = 28.93 ppm). Further fractionation of the methanolic extract led to the isolation of two principal alkaloids: carnegine and N-methylisosalsoline. These alkaloids are isoquinolines that have not previously been characterised for their molluscicidal activity. The N-methylisosalsoline possesses the highest molluscicidal activity (LC50 = 0.47 ìM against G. truncatula).


Assuntos
Animais , Alcaloides , Isoquinolinas , Moluscocidas , Extratos Vegetais , Plantas Medicinais , Caramujos/efeitos dos fármacos , Alcaloides/classificação , Alcaloides/isolamento & purificação , Isoquinolinas/classificação , Isoquinolinas/isolamento & purificação , Moluscocidas/química , Extratos Vegetais/análise , Extratos Vegetais/química , Folhas de Planta/química , Plantas Medicinais/química
5.
Acta Crystallogr D Biol Crystallogr ; 61(Pt 6): 784-8, 2005 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-15930640

RESUMO

Pressure is a non-invasive physical parameter that can be used to control and influence protein crystallization. It is also found that protein crystals of superior quality can be produced in gel. Here, a novel crystallization strategy combining hydrostatic pressure and agarose gel is described. Comparative experiments were conducted on hen and turkey egg-white lysozymes and the plant protein thaumatin. Crystals could be produced under up to 75-100 MPa (lysozymes) and 250 MPa (thaumatin). Several pressure-dependent parameters were determined, which included solubility and supersaturation of the proteins, number, size and morphology of the crystals, and the crystallization volume. Exploration of three-dimensional phase diagrams in which pH and pressure varied identified growth conditions where crystals had largest size and best morphology. As a general trend, nucleation and crystal-growth kinetics are altered and nucleation is always enhanced under pressure. Further, solubility of the lysozymes increases with pressure while that of thaumatin decreases. Likewise, changes in crystallization volumes at high and atmospheric pressure are opposite, being positive for the lysozymes and negative for thaumatin. Crystal quality was estimated by analysis of Bragg reflection profiles and X-ray topographs. While the quality of lysozyme crystals deteriorates as pressure increases, that of thaumatin crystals improves, with more homogeneous crystal morphology suggesting that pressure selectively dissociates ill-formed nuclei. Analysis of the thaumatin structure reveals a less hydrated solvent shell around the protein when pressure increases, with approximately 20% less ordered water molecules in crystals grown at 150 MPa when compared with those grown at atmospheric pressure (0.1 MPa). Noticeably, the altered water distribution is seen in depressurized crystals, indicating that pressure triggers a stable structural alteration on the protein surface while its polypeptide backbone remains essentially unaltered.


Assuntos
Muramidase/química , Proteínas de Plantas/química , Animais , Galinhas , Cristalização/métodos , Géis/química , Pressão , Perus
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