𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Enzymic properties of a mutant of Escherichia coli K 12 lacking nitrate reductase

✍ Scribed by Venables, W. A. ;Wimpenny, J. W. T. ;Cole, J. A.


Publisher
Springer-Verlag
Year
1968
Weight
278 KB
Volume
63
Category
Article
ISSN
0003-9276

No coin nor oath required. For personal study only.

✦ Synopsis


A pleiotropic mutant of Escherichia cell KI~ lacking reduced NAD: nitrate oxidoreductase, soluble formate dehydrogenase and membrane-bound formate:ferricytochrome b 1 oxidoreduetase is described. Levels of several other enzymes and cytochromes have been measured and found to differ little from those normally present in the wild type with the exceptions of eytoehrome c52~, reduced NAD:cytochrome e oxidoreductase and reduced NAD:nitrite oxidoreductase which are vel T high. Although the affected gene maps in a different position from that reported for chl A by other workers it seems likely that the two loci are identical.


πŸ“œ SIMILAR VOLUMES


Regulatory mutants of dihydrofolate redu
✍ Sheldon, Robert ;Brenner, Sydney πŸ“‚ Article πŸ“… 1976 πŸ› Springer 🌐 English βš– 668 KB

Trimethoprim inhibits dihydrofolate reductase. Mutations conferring trimethorpim-resistance on E coli K12 result in either an altered reductase with decreased affinity for the drug, or in 2-30 fold higher levels of the enzyme. Studies of the latter class of mutants indicate that dihydrofolate reduct

Assimilatory nitrate reductase in a chlo
✍ K. Motohara; Miya Kobayashi; Prof. Dr. M. Ishimoto πŸ“‚ Article πŸ“… 2007 πŸ› John Wiley and Sons 🌐 English βš– 550 KB

## Abstract Nitrate reductase was investigated in extracts from cells of a chlorate‐resistant mutant strain of __E. coli__ which grew anaerobically on nitrate as the sole source of nitrogen. The nitrate reductase was of particulate nature and reduced chlorate like the nitrate reductase from the wil

Altered dihydrofolate reductase in fol r
✍ Sheldon, Robert πŸ“‚ Article πŸ“… 1977 πŸ› Springer 🌐 English βš– 414 KB

Three spontaneous fol regulatory mutants contain dihydrofolate reductase molecules which differ in physical properties from enzymes of their parent strains. The enzymes were purified over 100-fold by affinity chromatography and were shown to differ in vitro in thermolability and in affinity for trim