PDF | In June , Jatropha gossypifolia (Euphorbiaceae) plants growing Article (PDF Available) · January with Reads Download full-text PDF. PDF | Extracts of J. gossypifolia L. have been reported to have several Ethanolic extract of Jatropha gossypifolia exacerbates Potassium Bromate- induced clastogenicity, hepatotoxicity, and lipid peroxidation in rats Download full-text PDF. Jatropha gossypiifolia L. (Euphorbiaceae), widely known as “bellyache bush,” is a medicinal plant largely used throughout Africa and. America.
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ABSTRACT. The present study deals with pharmacognostical and phytochemical evaluation of leaves of Jatropha gossypifolia L. Download PDFDownload Jatropha gossypiifolia L. (Euphorbiaceae) is popularly known as bellyache The medicinal tropic plant Jatropha gossypifolia L. fx1. Download high-res image (KB) · Download full-size image. Anti-inflammatory activity of leaves of Jatropha gossypifolia L. by hrbc membrane various extracts of Jatropha gossypifolia (J. gossypifolia). L. Thus human blood . publications. Total yearly downloads amount to million.
The genus comprises about species, most of them in warm temperate and subtropical regions and the seasonally dry tropics. Dehgan and Webster revised the subdivision made by Pax and now distinguish two subgenera Curcas and Jatropha of the genus Jatropha, with 10 sections and 10 subsections to accommodate the Old and New World species.
They postulated the physic nut Jatropha curcas L. Curcas Adans. Pax] to be the most primitive form of the Jatropha genus. Species in other sections evolved from the physic nut or another ancestral form, with changes in growth habit and flower structures. Hierarchical cluster analysis of 77 New World Jatropha species showed for the most part concordance with Dehgan and Webster's infrageneric classification Dehgan and Schutzman, Further cladistic analysis supported the Dehgan and Webster evolutionary model of the genus Jatropha.
Other Jatropha species in the section Curcas include: J. McVaugh considered J. One species, J. Two species, J. Inhibition of proteolytic activity upon azocasein The proteolytic activity of B. After 30 min standing at room temperature, the tubes were centrifuged at 8, g for 10 min. The supernatant was removed and mixed with 2 M NaOH. Blanks for each concentration were prepared the same way, except by adding the substrate only after trichloroacetic acid addition.
One Minimum Azocaseinolytic Concentration MAC was defined as the amount of venom able to produce a variation in absorbance of 0. Inhibition of fibrinogenolytic activity The fibrinogenolytic activity of B.
The enzymatic reaction was stopped by adding 1. Fibrinogen alone was also used as control, for visualization of the intact fibrinogen profile. Additionally, the fibrinogenolytic activity of B. Then, the samples were treated with Laemmli buffer in the absence of reducing agents, followed by room temperature incubation for 5 min.
After 3 washes with water for 5 min, the gels were stained with 0. Clear zones of substrate lysis against a blue background stain indicated presence of fibrinogenolytic enzymes. Molecular mass marker was used to estimate the approximate molecular mass of the fibrinogenolytic enzymes. Inhibition of procoagulant activity The procoagulant activity of B. Additionally, the anticoagulant activity of the extract, in absence of venom, was determined using the activated partial thromboplastin time aPTT and prothrombin time PT tests, as previously described in literature, with a few modifications .
In both tests, plasma alone was used as control absence of anticoagulant activity. Antioxidant activity evaluation The in vitro antioxidant activity of the aqueous leaf extract of J. Inhibition of phospholipase activity The phospholipase activity of B. After becoming solidified, holes of 0. Clear zones of substrate lysis halos against a yellow background indicated presence of phospholipase activity. One Minimum Phospholipase Concentration MPC was defined as the amount of venom able to produce a phospholipase halo of 25 mm.
Inhibition of defibrinogenating activity The defibrinogenating activity of B. Groups of 4 animals were treated with different doses of J. After 60 min, the animals received by intraperitoneal i.
The blood was placed in microtubes and left standing at room temperature for 60 min. The presence or absence of clotting formation after this period was registered. A group where animals received i. Another group that received i. Inhibition of local hemorrhagic activity The hemorrhagic activity of B.
Groups of 5 animals were treated with different doses of J. After 60 min, the animals received a subcutaneous s. After photo documentation of the hemorrhagic halos produced, the hemorrhagic skin was removed, weighted, fragmented and homogenized with water 1 mL of water for each mg of tissue. A group where animals received s. Another group that received s. Inhibition of edematogenic activity The edematogenic activity of B.
After 60 min, the animals received an intraplantar i. Edema was expressed as the percentage difference between the thickness of the paw after at respective times and before basal values venom injection. A group of animals that received i. Moreover, at the end of the experiment, the animals were sacrificed and their right hind paws were removed and analyzed for myeloperoxidase MPO activity, as previously described in literature, with a few modifications .
Tissues were homogenated in 0.
The left hind paws which did not received any treatment from venom control group were used as control basal values. The right paws of groups that received i. Inhibition of myotoxic activity The myotoxic activity of B. After 60 min, all the animals received an intramuscular i.
A group of animals received i. Interaction between extract and proteins The proteolytic action of the aqueous leaf extract from J.
Additionally, the protein precipitating action of the extract was evaluated using the Bradford dye-protein binding assay, as previously described in literature, with a few modifications . The supernatant obtained after centrifugation at 5, g for 15 min was mixed with Bradford reagent 0. Results and Discussion Phytochemical analysis of J. But first, the crude extract was fractionated by liquid-liquid partition to obtain fractions with different polarities and thus facilitating the chromatographic analysis of the compounds.
To the best of our knowledge, there are no phytochemical studies regarding the use of water as solvent for the extraction of J. This is important to be noted since popular use occurs more frequently with infusions or decoctions, and thus, little is known about the constitution of this kind of extract. Additionally, more commonly, the studies found in the literature use solvents or mixtures of solvents with non polar characteristic, which could contribute to further characterization of non-polar compounds, such as terpenoids and lignoids.
Isolation of polar compounds such as flavonoids, tannins and sugars are poorly described regarding the species so far  , . By co-TLC analysis, when considering the color developed by natural reagent A flavonoid specific reagent , Rf and spot overlap with standard, it was possible to suggest the presence of the flavonoids orientin, isoorientin, luteolin, vitexin and isovitexin in the extract.
With the exception of luteolin, the other flavonoids have already been identified in the leaves of J. For the genus Jatropha, luteolin was described previously only for the species Jatropha unicostata . Additionally, the content of sugar, phenolic compounds and proteins quantified were So, the presence of phenolic compounds and sugars could be confirmed and it could be visualized that proteins represent only a small percentage of the crude extract composition.
The presence of flavonoids and tannins could be especially interesting in antiophidic plants since flavonoids are able to promote strong hydrogen bonds with amides of protein chains and exhibit metal chelating activity and tannins have the ability to precipitate proteins . The flavonoid luteolin, for example, as previously described in literature, presents inhibitory action against hyaluronidases from Crotalus adamenteus snake venom . Cytotoxicity assays of J.
These results may suggest that the aqueous extract of the leaves, compared to the ethanol extract of the aerial parts tested by Mariz et al.
In fact, a study investigating the acute oral toxicity of an aqueous leaf extract of J. However, it is important to note that the toxicity of the aqueous leaf extract of J.
Antiophidic activity evaluation of J. However, studies that evaluate the antiophidic activity of Jatropha species are very scarce in the literature.
Only some studies have shown the antiophidic properties of Jatropha elliptica and Jatropha mollissima, with interesting results, according to the venom tested  , . However, studies showing the antiophidic activity of J. In view of this and the popular use of the plant, this species was chosen as object of this study.
Thus, inhibition of proteolytic enzymes is important when thinking about molecules with antiophidic activity. Snake venoms are rich in several proteolytic enzymes that degrade a wide variety of natural substrates, such as casein, fibrinogen and collagen, among others. It is known that several hemorrhagic and defibrinogenating toxins in snake venoms show significant activity against these substrates .