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

FEBS Letters

Then, Rudolf L.¹  Hartman, Peter G.¹  Kocher, Hans P.¹  Stähli, Marija¹ 

[1] Pharmaceutical Research Department, F. Hoffmann-La Roche & Co. Ltd, CH-4002 Basel, Switzerland

关键词: Trimethoprim resistance;    Dihydrofolate reductase;    Amino acid sequence;    (Staphylococcus aureus);   

DOI  :  10.1016/0014-5793(88)81006-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown