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Snake venom phospholipases A₂ (PLA₂) share high sequence identities and a conserved structural scaffold, but show important functional differences. Only a few PLA₂s have been purified and characterized from coral snake (Micrurus spp.) venoms, and their role in envenomation remains largely unknown. In this report, we describe the isolation, sequencing and partial functional characterization of two Micrurus PLA₂s: MmipPLA₂ from Micrurus mipartitus and MdumPLA₂ from Micrurus dumerilii, two species of clinical importance in Colombia. MmipPLA₂ consisted of 119 amino acid residues with a predicted pI of 8.4, whereas MdumPLA₂ consisted of 117 residues with a pI of 5.6. Both PLA₂s showed the conserved 'group I' cysteine pattern and were enzymatically active, although MdumPLA₂ had higher activity. The two enzymes differed notably in their toxicity, with MmipPLA₂ being highly lethal to mice and mildly …