The expression of the recombinant Crotalus atrox Snake venom serine protease catroxase-2 involves the construction of a plasmid encoding the Crotalus atrox Snake venom serine protease catroxase-2 (25-258aa) and the N-terminal 6xHis-tag. This resulting plasmid is introduced into yeast cells. Positive yeast cells are selected and cultured for protein expression. After that, cultured cells are lysed. The subsequent step includes purifying the recombinant Crotalus atrox Snake venom serine protease catroxase-2 protein through affinity purification from the cell lysate and assessing the purity of the protein via SDS-PAGE. The purity of the recombinant Snake venom serine protease catroxase-2 is greater than 85%.
Snake venom serine proteases (SVSPs) are key players in snake venom, especially in viperid snakes, and are central to how venom works. They belong to a group of enzymes called the S1 family of serine proteinases and come in various sizes, typically between 26 and 67 kilodaltons, with two distinct structural parts [1]. These enzymes mess with the body's blood clotting system in several ways, like breaking down fibrinogen and activating protein C into activated protein C [2][3][4]. One reason they're so effective is that they remain stable across a wide range of pH levels, which helps them do their job well in an envenomation [5]. Even though SVSPs look similar at the amino acid level, they can have different jobs and targets, indicating they're not all the same [6]. By breaking down fibrin(ogen), SVSPs prevent blood from clotting, making it easier for other toxins in the venom to spread throughout the victim's body [3]. Scientists are interested in SVSPs for drug development, especially for making antivenoms [1]. They're also looking into the three-dimensional structures of SVSPs, hoping to find clues for new medicines [7]. Overall, SVSPs are crucial components of snake venom, causing complex effects in envenomations and offering potential opportunities for treatments.
References:
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