Thermal transition of a mutated dihydrofolate reductase
β Scribed by H. Uedaira; S. Kidokoro; M. Iwakura; S. Honda; S. Ohashi
- Publisher
- Elsevier Science
- Year
- 1990
- Tongue
- English
- Weight
- 377 KB
- Volume
- 163
- Category
- Article
- ISSN
- 0040-6031
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Folate was coupled t,o AH-Sepharose 4B, the gel poured into small columns, and the Sepharose-bound folate reduced in situ to dihydrofolate by dithionite/ascorbate at pH 6 to 7. The dihydrofolate-Sepharose column was used to purify guanosine triphosphate cyclohydrolase I (EC 3.5.4.16) and dihydrofola
Two site-specific mutations of dihydrofolate reductase from Escherichiu coli based on the x-ray crystallographic structure were constructed. The first mutation (His-45 + Gln) is aimed at assessing the interaction between the imidazole moiety and the pyrophosphate backbone of NADPH. The second (Thr-1
We have previously demonstrated systemic resistance to methotrexate (MTX) in transgenic mice carrying a foreign, mutant dihydrofolate reductase (DHFR, E.C. 1 S.1.3) gene. The new gene was introduced as a cDNA cloned into an expression vector driven by the simian virus 40 (SV40) early promoter. Previ
We have employed deuterium NMR techniques to determine the dynamics of trimethoprim (TMP) in a binary complex with dihydrofolate reductase (DHFR) or in a ternary complex with DHFR and cofactor NADP+ in the fully hydrated state. TMP was deuterated at the following positions: (2',6'-D2)TMP, (3'-Ome-D3