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1: FEBS Lett. 1988 Dec 19;242(1):157-60.Click here to read Links

N-terminal amino acid sequence of the chromosomal dihydrofolate reductase purified from trimethoprim-resistant Staphylococcus aureus.

Hartman PG, Stähli M, Kocher HP, Then RL.

Pharmaceutical Research Department, F. Hoffmann-La Roche & Co. Ltd, Basel, Switzerland.

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.

PMID: 3060373 [PubMed - indexed for MEDLINE]

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