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1.
Rev. bras. farmacogn ; 19(4): 893-897, out.-dez. 2009. ilus, tab
Artigo em Português | LILACS | ID: lil-542705

RESUMO

O estudo fitoquímico do extrato etanólico das folhas de Moringa oleifera Lam., Moringaceae, resultou no isolamento dos derivados benzilnitrilas niazirina, niazirinina e 4-hidroxifenil-acetonitrila, enquanto que das cascas dos frutos somente o octacosano foi obtido. Os óleos essenciais das folhas, flores e frutos foram analisados por cromatografia gasosa acoplada a espectrometria de massa. Os constituintes principais identificados foram: fitol (21,6 por cento) e timol (9,6 por cento) nas folhas, octadecano (27,4 por cento) e ácido hexadecanóico (18,4 por cento) nas flores e docosano (32,7 por cento) e tetracosano (24,0 por cento) nos frutos. As estruturas dos compostos isolados foram identificadas a partir de técnicas espectroscópicas (RMN, IV e EM). A 4-hidroxifenil-acetonitrila está sendo citada pela primeira vez para o gênero Moringa e os óleos essenciais das flores e frutos estão sendo citados pela primeira vez para a espécie M. oleifera.


Phytochemical analysis of the ethanol extract from leaves of Moringa oleifera Lam., Moringaceae, yield the benzylnitriles: niazirine, niazirinine and 4-hydroxyphenylacetonitrile, while of fruit shells only octacosane was isolated. The essential oils from leaves, flowers and fruits were examined by gas chromatography-mass spectrometry. The major constituents identified were: phytol (21.6 percent) and thymol (9.6 percent) in the leaves oil, octadecane (27.4 percent) and hexadecanoic acid (18.4 percent) in the flowers oil, docosane (32.7 percent) and tetracosane (24.0 percent) in the fruits oil. The structures of all compounds were identified by spectroscopic analyses (NMR, IR and MS). 4-hydroxyphenylacetonitrile is reported for the first time to the Moringa genus and the essential oils of flowers and fruits are reported for the first time to the species M. oleifera.

2.
Rev. bras. farmacogn ; 19(2b): 586-591, abr.-jun. 2009. tab
Artigo em Português | LILACS | ID: lil-531828

RESUMO

Caesalpinia ferrea Mart. (jucá ou pau-ferro) é uma espécie da família Leguminosae cuja ocorrência estende-se da região Nordeste ao Estado do Rio de Janeiro. Trata-se de uma espécie bastante utilizada na medicina popular pelas suas inúmeras propriedades terapêuticas tais como antiinflamatória, analgésica, antimicrobiana e antitérmica as quais indicam a presença de compostos de interesse farmacológico. Contudo, muitos estudos em plantas também investigam a presença de compostos de interesse industrial. Com base nas propriedades terapêuticas e atividades já descritas para essa espécie, esse trabalho objetivou pesquisar atividades biológicas no extrato de sementes de C. ferrea na busca por compostos de interesse industrial e farmacológico. Os resultados indicaram a presença das atividades celulásica, amilásica, anticoagulante e larvicida contra A. aegypti no extrato aquoso das sementes de C. ferrea, entretanto, não foram observadas as atividades tóxica aguda, hemolítica, heparinásica, antibacteriana e antifúngica.


Caesalpinia ferrea Mart. is a species belonging to Leguminosae family commonly known in Brazil as "jucá" or "pau-ferro". It occurs in Brazil from the Northeast Region to the State of Rio de Janeiro and it is widely utilized in folk medicine due to its several therapeutic properties such as anti-inflammatory, analgesic, antimicrobial and antithermic, which indicate the presence of compounds of pharmacological interest. Besides, many studies with plants look for the presence of compounds with industrial applications. Based upon the therapeutic and bioactive properties described for this species so far, this work aimed to investigate several biological activities in the water extract of C. ferrea seeds. The results indicated the presence of the following activities: cellulase, amylase, anticoagulant and larvicide against A. aegypti in the water extract of C. ferrea seeds. Nevertheless, the extract did not show the other activities assayed: acute toxic activity, hemolytic, heparinasic, antibacterial and antifungal activities.

3.
Phytochemistry ; 65(1): 59-69, 2004 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-14697271

RESUMO

The complete sequences of nuclear ribosomal DNA (nrDNA) internal transcribed spacer regions (ITS/5.8S) were determined for species belonging to six genera from the subtribe Diocleinae as well as for the anomalous genera Calopogonium and Pachyrhizus. Phylogenetic trees constructed by distance matrix, maximum parsimony and maximum likelihood methods showed that Calopogonium and Pachyrhizus were outside the clade Diocleinae (Canavalia, Camptosema, Cratylia, Dioclea, Cymbosema, and Galactia). This finding supports previous morphological, phytochemical, and molecular evidence that Calopogonium and Pachyrhizus do not belong to the subtribe Diocleinae. Within the true Diocleinae clade, the clustering of genera and species were congruent with morphology-based classifications, suggesting that ITS/5.8S sequences can provide enough informative sites to allow resolution below the genus level. This is the first evidence of the phylogeny of subtribe Diocleinae based on nuclear DNA sequences.


Assuntos
DNA Ribossômico/genética , Fabaceae/genética , Algoritmos , Sequência de Bases , Núcleo Celular/genética , Sequência Consenso , DNA de Plantas/genética , Fabaceae/classificação , Dados de Sequência Molecular , Filogenia , Alinhamento de Sequência , Homologia de Sequência do Ácido Nucleico , Transcrição Gênica
4.
Phytochemistry ; 61(3): 301-10, 2002 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-12359516

RESUMO

A lectin was purified from the cotyledons of Luetzelburgia auriculata (Fr. All) Ducke by affinity chromatography on agarose-N-acetyl-D-galactosamine. The lectin is a potent agglutinin for rabbit erythrocytes, reacts with human red cells, but is inactive against cow, sheep, and goat erythrocytes. Hemagglutination of rabbit erythrocytes was inhibited by either 0.39 mM N-acetyl-neuraminic acid or N-acetyl-D-galactosamin, 12.5 mM D-lactose or D-melibiose, 50 mM D-galactose or raffinose. Its hemagglutinating activity was lost at 80 degrees C, 5 min, and the activation energy required for denaturation was 104.75 kJ mol(-1). Chromatography on Sephadex G-100, at pH 7.6, showed that at this hydrogenic ionic concentration the native lectin was a homotetramer (123.5 kDa). By denaturing SDS-PAGE, LAA seemed to be composed of a mixture of 29 and 15 kDa polypeptide subunits. At acidic and basic pHs it assumed different conformations, as demonstrated by exclusion chromatography on Superdex 200 HR 10/30. The N-terminal sequence of the 29 kDa band was SEVVSFSFTKFNPNQKDII and the 15 kDa band contained a mixture of SEVVSFSFTKFNPNQKDII and KFNQIVAVEEDTDXESQPQ sequences, indicating that these bands may represent full-length and its endogenous fragments, respectively. The lectin is a glycoprotein having 3.2% neutral carbohydrate, with a pI of 5.8, containing high levels of Asp+Asn and Glu+Gln and hydroxy amino acids, and low amount or absence of sulfur amino acids. Its absorption spectrum showed a maximum at 280 nm and a epsilon (1%) x (1cm) of 5.2. Its CD spectrum was characterized by minima near 228 nm, maxima near 196 nm and a negative to positive crossover at 210 nm. The secondary structure content was 6% alpha-helix, 8% parallel beta-sheet, 38% antiparallel beta-sheet, 17% beta-turn, 31% unordered and others contribution, and 1% RMS (root mean square). In the fluorescence spectroscopy, excitation of the lectin solution at 280 nm gave an emission spectrum in the 285-445 nm range. The wavelength maximum emission was in 334.5 nm, typical for tryptophan residues buried inside the protein.


Assuntos
Fabaceae/química , Lectinas/química , Lectinas/isolamento & purificação , Sequência de Aminoácidos , Aminoácidos/análise , Carboidratos/análise , Cromatografia por Troca Iônica , Dicroísmo Circular , Eletroforese em Gel de Poliacrilamida , Hemaglutinação , Temperatura Alta , Concentração de Íons de Hidrogênio , Focalização Isoelétrica , Lectinas/metabolismo , Dados de Sequência Molecular , Peso Molecular , Análise de Sequência de Proteína
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