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Some are strongly peroxide-dependent and possess very low antibacterial action when treated with catalase to remove peroxide activity [ 3, 4, 7].
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A Carulite-200® catalyst was used to remove peroxides from ambient air to blank the system to account for variations in the ambient air matrix.
Membrane-anchored proteins, antioxidant AhpC/TSA family, have antioxidant activity that could remove peroxides or H2O2.
Subsequently, ascorbate peroxidase (#116) removes peroxide and generates monodehydrodoascorbate, which is then reduced by monodehydroascorbate reductase (#119) [ 75, 76].
Damage to these enzymes may play a major role in altering the redox balance within cells as TrxR is critical to the maintenance of thioredoxin in its reduced form, with this in turn being a key co-factor for the peroxiredoxin family of enzymes, which play a critical role in removing peroxides (H2O2 [ 11] and also amino acid/protein hydroperoxides [ 43]) from cells.
Treating MEU with alumina to remove the peroxide reduced the concentration of peroxide but did not eliminate it.
Catalase (CAT) could decompose hydrogen peroxide into water and oxygen to remove the peroxide in plants, and the higher activity of CAT was, the stronger salt tolerance would be (Ho et al. [1998]).
Peroxides are considered to be pathogen responsive and remove hydrogen peroxide from the cell (reviewed in [ 103]).
On addition of peroxide to oxidised enzyme in the presence of catalase (to remove excess peroxide within a few seconds) there is immediate formation of an initial compound P species which changes to give largely compound F over a period of tens of seconds.
The combined action of these enzymes to remove hydrogen peroxide and superoxide is important because these by-products together with iron form the extremely reactive hydroxyl radical, which is capable of killing the cell.
StyB reductase, formate, formate dehydrogenase and catalase were added in order to produce reduced FAD, regenerate NADH, and remove hydrogen peroxide.
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