We have cloned, over-expressed and purified enolase from Plasmodium falciparumstrain NF54 in Escherichia coliin active form, as an N-terminal His6-tagged protein. The sequence of the cloned enolase from the NF54 strain is identical to that of strain 3D7 used in full genome sequen-cing. The recombinant enolase (r-Pfen) could be obtained in large quantities ( 50 mg per litre of culture) in a highly purified form ( 95%). The purified protein gave a single band at 50 kDa on SDS/PAGE. MALDI-TOF analysis gave a mean ± SD mass of 51396 ± 16 Da, which is in good agreement with themass calculated fromthe sequence
