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Fig. 1 | Journal of Venomous Animals and Toxins including Tropical Diseases

Fig. 1

From: Biochemical characterization of a phospholipase A2 homologue from the venom of the social wasp Polybia occidentalis

Fig. 1

Purification of PocTX. a P. occidentalis venom (100 mg) was applied to a Sephacryl S200 column, pre-equilibrated with sodium bicarbonate buffer. The eluted fractions were analyzed with 12.5% 1D SDS-PAGE electrophoresis to check the separation profile, where a predominance of relative masses was observed at 65 kDa and 14 kDa. b Next, the fractions (10 μg) were tested for their phospholipase activity, among which P1, P2, P3 and P4 had activity on the substrate 4N3OBA. c These fractions were mixed and rechromatographed on a reverse phase column, with the elution of two fractions (F1 and F2); upon analysis of the purity of the eluted fractions with 12.5% 1D SDS-PAGE, it was found that one of them showed a single protein band at approximately 14 kDa. The gels were stained with Coomassie Blue G250. The results were expressed as mean ± standard deviation (n = 3) and submitted to variance analysis followed by the Tukey posttest. *Significant values when compared to the control groups (p < 0.05). C+: positive control – Bothrops jararacussu venom. C-: negative control – distilled water

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