SUMMARY: We have shown by appropriate modification of the translational signals and using the strong T7 RNA polymerase promoter ·10, that a cloned pyruvate decarboxylase gene () can be expressed in This protein, which migrated as a single band on SDS-polyacrylamide gels, was found to have a subunit molecular mass of approximately 62 kDa, similar to that of the enzyme produced by yeast. Polyclonal antibodies raised against purified yeast pyruvate decarboxylase recognized this bacterially produced protein. We found that this recombinant enzyme is active, indicating that the homotetramer encoded by the gene is functional.


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