Abstract
Two-dimensional gel electrophoresis (2DE) in polyacrylamide was used to map the proteins in lysates of the archaeon (formerly archaebacterium) Pyrococcus furiosus and to analyze enzymes purified from P. furiosus. The location of the enzymes in the 2DE maps was determined by comigration of lysate proteins with purified enzymes. A 2DE map of P. furiosus proteins with some identifications was produced, which will be useful for future studies of protein expression in this organism. In addition, the usefulness of 2DE for evaluating the purity of enzyme preparations and for characterizing their subunit structure under denaturing conditions was investigated.
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