N-terminal amino acid sequence of the chromosomal dihydrofolate reductase purified from trimethoprim-resistant Staphylococcus aureus |
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| Authors: | P G Hartman M St?hli H P Kocher R L Then |
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| Affiliation: | Pharmaceutical Research Department, F. Hoffmann-La Roche & Co. Ltd, Basel, Switzerland. |
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| Abstract: | The existence of two distinct dihydrofolate reductases (DHFR) in highly trimethoprim-resistant clinical isolates has been unequivocally demonstrated. The enzymes have been characterized with regard to the affinity for substrates and sensitivity to inhibitors. The chromosomal, trimethoprim-sensitive DHFR was purified to homogeneity by a new simple two-step procedure. Its N-terminal amino acid sequence, determined up to the first 35 amino acids, showed 69% homology with the Escherichia coli DHFR. |
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