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This work reports the purification and biochemical and functional characterization of ACP-TX-I and ACP-TX-II, two phospholipases A 2 (PLA 2 ) from Agkistrodon contortrix pictigaster venom. Both PLA 2 s were highly purified by a single chromatographic step on a C 18 reverse phase HPLC column. Various peptide sequences from these two toxins showed similarity to those of other PLA 2 toxins from viperid snake venoms. ACP-TX-I belongs to the catalytically inactive K49 PLA 2 class, while ACP-TX-II is a D49 PLA 2 , and is enzymatically active. ACP-TX-I PLA 2 is monomeric, which results in markedly diminished myotoxic and inflammatory activities when compared with dimeric K49 PLA 2 s, confirming the hypothesis that dimeric structure contributes heavily to the profound myotoxicity of the most active viperid K49 PLA 2 s. ACP-TX-II exhibits the main pharmacological actions reported for this protein family, including in vivo local myotoxicity, edema-forming activity, and in vitro cytotoxicity. ACP-TX-I PLA 2 is cytotoxic to A549 lung carcinoma cells, indicating that cytotoxicity to these tumor cells does not require enzymatic activity.

toxins

ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional Characterization