Abstract
A cDNA encodingBungarus multicinctus(Taiwan banded krait) phospholipase A2was expressed inEscherichia coli.The expressed PLA2contained a Met residue fused to the N-terminus of PLA2. The expressed protein was isolated from inclusion bodies ofE. coliand subjected to refolding into its folded structure. Then the N-terminus Met residue of recombinant PLA2was cleaved with aminopeptidase. The resulting recombinant PLA2had the same amino acid composition and N-terminal sequence of native PLA2and displayed the same CD spectra and pI value as native enzyme. Moreover, the recombinant PLA2was indistinguishable from native PLA2in enzymatic activity and antigenicity. These results suggest that a fully active PLA2enzyme has been successfully expressed as its native form in snake venom.
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