Snake venoms are complex mixtures of proteins and polypeptides responsible for immobilization, death and digestion of the prey. Although snake venoms have been deeply studied, there are still some toxins with functions not fully elucidated, such as L-amino acid oxidases (SV-LAAOs). It is known that several factors influence the composition of the snake venoms. Geographic distribution, feeding habits, ontogenetic development, seasonal variations and even the frequency of extractions are some of the factors that contribute to the intraspecific variation of snake venoms. In a previous study carried out by our group, it was observed some differences between venoms collected from individuals in different environments (nature and captivity) belonging to the subspecies Crotalus durissus terrificus. The results of this study demonstrated that the venom of most of the snakes kept in captivity showed a yellow color, while the predominant color of the venoms of recently wild-caught specimens is white. This color difference showed a correlation with the higher SV-LAAO activity in the yellow-colored venom from captive snakes. By polyacrylamide gel electrophoresis (PAGE) it was observed that the venoms collected from snakes kept in captivity present a band of approximately 60 kDa that is absent or less abundant in the venom of recently wild-caught individuals. This protein band was identified by mass spectrometry as being, in fact, a SV-LAAO. Thus, the objective of this work is to qualitatively and quantitatively analyze the LAAO enzyme in the venom of C. durissus terrificus snakes born and/or kept in captivity in the Herpetology Laboratory of the Butantan Institute and recently wild-caught.
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