Article
Trimethoprim resistance in Haemophilus influenzae is due to altered dihydrofolate reductase(s).
The Biochemical journal - 15 Mar 1991
de Groot R, Chaffin D O, Kuehn M, Smith A L
Abstract excerpt
We characterized a highly purified preparation of the chromosomally encoded dihydrofolate reductase (DHFR) from a trimethoprim-susceptible (Tmp8; strain MAP) and two trimethoprim-resistant (TmpR) strains (MAP/47 and MAP/42) of Haemophilus influenzae. The enzymes were purified between 650- and 3000-fold by gel-filtration and dye-ligand chromatography. The apparent molecular mass of the three proteins was 18400 Da...
Topics
- Chromatography, Gel
- Drug Resistance
- Electrophoresis, Polyacrylamide Gel
- Haemophilus influenzae
- Isoelectric Focusing
- Kinetics
- Mutation
- Peptide Mapping
- Tetrahydrofolate Dehydrogenase
- Trimethoprim