Navegando por Autor "Oliveira, Adeliana"
Agora exibindo 1 - 4 de 4
- Resultados por página
- Opções de Ordenação
Artigo Activity toward bruchid pest of a kunitz-type inhibitor from seeds of the algaroba tree (prosopis juliflora D.C.)(Pesticide Biochemistry and Physiology, 2002) Morais, Ana Heloneida de Araújo; Oliveira, Adeliana; Pereira, Railene; Lima, Liziane; Franco, Octávio Luiz; Bloch Júnior, Carlos; Sá, Maria Fátima Grossi de; Sales, MaurícioA proteinaceous inhibitor with high activity against papain was found in seeds of the xerophytic algaroba tree (Prosopis julifora). The proteinase inhibitor Pj was purified using Sephacryl S-200 gel filtration followed by reverse-phase high-performance liquid chromatography on a Vidac 18 TP. Inhibitor Pj showed a Mr of 20,000 on sodium dodecyl sulfate–polyacrylamide gel electrophoresis and a Mr of 19.2K by mass spectrometry. The inhibition of papain by the Pj inhibitor was the noncompetitive type, with a Ki value of 0.59 3 1029 M. The gelatinase activity of papain was strongly inhibited by Pj too. The N-terminal amino acid sequence of the Pj inhibitor showed homology with the N-terminal amino acid sequence of the Kunitzproteinase inhibitor family. Pj was strongly effective against digestive proteinases from bean weevil Acanthoscelides obtectus and cowpea weevil Callosobruchus maculatus and was moderately active toward midgut proteinases from pod weevil Mimosestes mimosae and Mexican bean weevil Zabrotes subfasciatus. The data shown here suggest that the protein present in algaroba seeds is involved with defense responses to insects and may be an important tool to be used in engineering plants resistant to bean weevilArtigo Characterization and pharmacological properties of a novel multifunctional kunitz inhibitor from erythrina velutina seeds(PloS One, 2013-05) Morais, Ana Heloneida de Araújo; Machado, Richele Janaína Araújo; Monteiro, Norberto de Kássio Vieira; Migliolo, Ludovico; Silva, Osmar Nascimento; Pinto, Michele Flaviane Soares; Oliveira, Adeliana; Franco, Octávio Luiz; Kiyota, Sumika; Bemquerer, Marcelo Porto; Uchôa, Adriana Ferreira; Santos, Elizeu Antunes dosInhibitors of peptidases isolated from leguminous seeds have been studied for their pharmacological properties. The present study focused on purification, biochemical characterization and anti-inflammatory and anticoagulant evaluation of a novel Kunitz trypsin inhibitor from Erythrina velutina seeds (EvTI). Trypsin inhibitors were purified by ammonium sulfate (30–60%), fractionation followed by Trypsin-Sepharose affinity chromatography and reversed-phase high performance liquid chromatography. The purified inhibitor showed molecular mass of 19,210.48 Da. Furthermore, a second isoform with 19,228.16 Da was also observed. The inhibitor that showed highest trypsin specificity and enhanced recovery yield was named EvTI (P2) and was selected for further analysis. The EvTI peptide fragments, generated by trypsin and pepsin digestion, were further analyzed by MALDI-ToF-ToF mass spectrometry, allowing a partial primary structure elucidation. EvTI exhibited inhibitory activity against trypsin with IC50 of 2.261028 mol.L21 and constant inhibition (Ki) of 1.061028 mol.L21 , by a non-competitive mechanism. In addition to inhibit the activity of trypsin, EvTI also inhibited factor Xa and neutrophil elastase, but do not inhibit thrombin, chymotrypsin or peptidase 3. EvTI was investigated for its anti-inflammatory and anticoagulant properties. Firstly, EvTI showed no cytotoxic effect on human peripheral blood cells. Nevertheless, the inhibitor was able to prolong the clotting time in a dose-dependent manner by using in vitro and in vivo models. Due to antiinflammatory and anticoagulant EvTI properties, two sepsis models were here challenged. EvTI inhibited leukocyte migration and specifically acted by inhibiting TNF-a release and stimulating IFN-a and IL-12 synthesis. The data presented clearly contribute to a better understanding of the use of Kunitz inhibitors in sepsis as a bioactive agent capable of interfering in blood coagulation and inflammationArtigo In vitro digestibility of globulins from cowpea (vigna unguiculata) and xerophitic algaroba (prosopis juliflora) seeds by mammalian digestive proteinases: a comparative study(Food Chemistry, 2002) Morais, Ana Heloneida de Araújo; Oliveira, Adeliana; Lima, Liziane; Pereira, Railene; Cardoso, Patrícia; Miranda, Maria Raquel; Sales, Maurício; Xavier Filho, JoséGlobulins were purified from mature and immature cowpea and algaroba seeds by gel filtration (S-200), anion exchange (DEAE-Sepharose) and other chromatographic methods. These globulins (native and heated) were submitted to hydrolysis by pepsin, chymotrypsin and trypsin and their digestion products were analysed by SDS-PAGE. Results showed that native globulins of both legumes were weakly digested by pepsin and were not digested by serine proteases. Heated proteins from cowpea were digested more rapidly by pepsin and chymotrypsin than was algaroba globulin. Trypsin rapidly digested proteins from both cowpea and algaroba. Comparing the hydrolysis of bean globulins to the algaroba globulins by mammalian enzymes, the globulins from immature cowpea showed better digestibility than mature cowpea; globulins from algaroba pod, which is used as an alternative food, were difficult to digestArtigo The performance of callosobruchus maculatus F. in artificial seeds containing proteins from prosopis juliflora seeds(Protein and Peptide Letters, 2001) Morais, Ana Heloneida de Araújo; Oliveira, Adeliana; Lima, Liziane; Pereira, Pereira; Sales, MaurícioThis work reportes the effects of isolated proteins from algaroba (Prosopis juliflo ra D.C.) seeds fractionated by ammonium sulfate at saturation 0-30percent., 30-60percent and 60-90percent. They were tested, in vitro, against papain and midgut homogenate of C. maculatus larvae. Also, the effects in vivo these protein fractions on the development of C. maculatus larvae were tested. F 30 / 60 fraction was effective against papain (72percent inhibition), midgut homogenate of larvae of C. maculatus (59,2percent inhibition) and in vivo with WD50 of 1,7percent