sepharose and Edema

The lectin from Platypodium elegans seeds (PELa) was purified by affinity chromatography in a mannose-agarose column. The lectin agglutinated rabbit erythrocytes and the agglutinating effect was inhibited by previous incubation with the glycoprotein fetuin, along with N-acetyl-d-glucosamine, D-mannose and its derivatives. The lectin maintained complete activity in temperatures ranging from 40 to 60°C and pH values ranging from 9 to 10. As a glycoprotein, PELa has a carbohydrate content of 2.2%, and its activity requires divalent cations such as Ca

Topics: Animals; Edema; Erythrocytes; Fabaceae; Hemagglutination; Immobilized Proteins; Male; Plant Lectins; Rabbits; Rats; Recombinant Proteins; Seeds; Sepharose

In the present study, an acidic PLA(2), designated Bl-PLA(2), was isolated from Bothrops leucurus snake venom through two chromatographic steps: ion-exchange on CM-Sepharose and hydrophobic chromatography on Phenyl-Sepharose. Bl-PLA(2) was homogeneous on SDS-PAGE and when submitted to 2D electrophoresis the molecular mass was 15,000Da and pI was 5.4. Its N-terminal sequence revealed a high homology with other Asp49 acidic PLA(2)s from snake venoms. Its specific activity was 159.9U/mg and the indirect hemolytic activity was also higher than that of the crude venom. Bl-PLA(2) induced low myotoxic and edema activities as compared to those of the crude venom. Moreover, the enzyme was able to induce increments in IL-12p40, TNF-α, IL-1β and IL-6 levels and no variation of IL-8 and IL-10 in human PBMC stimulated in vitro, suggesting that Bl-PLA(2) induces proinflammatory cytokine production by human mononuclear cells. Bothrops leucurus venom is still not extensively explored and knowledge of its components will contribute for a better understanding of its action mechanism.

Topics: Amino Acid Sequence; Animals; Bothrops; Cells, Cultured; Chromatography, Ion Exchange; Crotalid Venoms; Cytokines; Edema; Electrophoresis, Polyacrylamide Gel; Humans; Inflammation; Interleukin-10; Interleukin-12 Subunit p40; Interleukin-6; Interleukin-8; Leukocytes, Mononuclear; Male; Mice; Molecular Weight; Phospholipases A2; Sepharose; Sequence Homology, Amino Acid; Tumor Necrosis Factor-alpha

Porphyran is a major component of the red algae, Porphyra tenera and P. yezoensis, which are processed into a sheet type of dried food, "Nori". Porphyran has been reported to activate murine macrophages by in vitro and i.p. injection studies. The contact hypersensitivity (CHS) reaction in mice is commonly used as a model to evaluate the anti-allergic activity of food and food components. We therefore studied the effect of porphyran on the CHS reaction in Balb/c mice to evaluate anti-allergic activity of porphyran. We found that an oral administration of porphyran (2% in drinking water) suppressed the CHS reaction (ear edema) induced by 2,4,6-trinitrochlorobenzene. We also found that porphyran suppressed the serum level of IgE and the production of interferon-gamma (IFN-gamma) in the challenged ear lobe. We conclude from these results that the CHS reaction was suppressed by oral porphyran due to the decreased serum level of IgE and the production of IFN-gamma in the challenged ear lobe.

Topics: Animals; Anti-Allergic Agents; Dermatitis, Contact; Ear; Edema; Immunoglobulin E; Immunosuppression Therapy; Interferon-gamma; Mice; Mice, Inbred BALB C; Picryl Chloride; Porphyra; Sepharose

The effect of locally applied calcium on the vascular permeability is studied under the conditions of an acute inflammatory reaction. Using the Sephadex-inflammation, local elevated calcium concentration neither inhibited oedema formation, nor were reduction of inflammatory signs at all observed on the microscopical level.

Topics: Animals; Calcium; Capillary Permeability; Edema; Inflammation; Rats; Sepharose