Snake venoms present a wide range of components able to induce various pathological symptoms in victims of envenoming, which is part of the neglected circumstances by WHO and is a serious public health problem in Brazil. Snakes of Crotalus durissus species represent Crotalus genus in the national territory. Crotalus durissus collilineatus venom presents a great complexity of protein components, which contribute to the toxic effects observed in the crotalic accident. However, due to its complexity, many components have not yet been isolated, as phosphodiesterase (PDE). These enzymes are part of the nucleases, such as DNAse and RNAse, and have a high molecular mass (90 ~160 kDa), being found in monomeric or dimeric forms. PDEs are responsible for the cleavage of phosphodiester bonds of nucleic acids, ATP, ADP, NAD, NGD, cAMP and cGMP, being able to interfere in physiological or pathological processes, which make them therapeutic targets of various diseases. Their role in the snakebite envenoming is still not fully elucidated, but it is known that PDEs are capable to leading to hypotension and locomotor depression of the prey and they are also capable of inhibiting platelet aggregation in vitro. Therefore, the objectives of this study are to determine the molecular mass of PDE from C. d. collilineatus venom, its full amino acid sequence, using a multi enzymatic limited digestion, and its glycosylation pattern, showing glycosylation sites and carbohydrate composition. All of these assays will be performed by mass spectrometry techniques. In this way, the present study becomes relevant because will analyze structurally a toxin that is important for snakebite envenoming, but still little studied, increasing the knowledge about this protein and its enzymatic class.
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