ArticleThe journal of venomous animals and toxins including tropical diseases2018
Biochemical characterization of a phospholipase A
Article in The journal of venomous animals and toxins including tropical diseases, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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11 authors at 2 institutions in 1 country.
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Abstract
backgroundWasp venoms constitute a molecular reservoir of new pharmacological substances such as peptides and proteins, biological property holders, many of which are yet to be identified. Exploring these sources may lead to the discovery of molecules hitherto unknown. This study describes, for the first time in hymenopteran venoms, the identification of an enzymatically inactive phospholipase A
methods
resultsThe protein, called PocTX, was isolated using two chromatographic steps. Based on the phospholipase activity assay, electrophoresis and mass spectrometry, the protein presented a high degree of purity, with a mass of 13,896.47 Da and a basic pI. After sequencing by the Edman degradation method, it was found that the protein showed a high identity with snake venom PLA
conclusionThis is the first report of an enzymatically inactive PLA
Indexed as
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