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Some of the enzymes possibly associated with PPO activation have been listed above in the Enzyme section.
In the Varying HCO 3 − transport saturates enzyme section we had: The chemical equilibrium is K e q = H / C = (K b a V c a ) (K c a V b a ) ≈ 5, for pH around 7 (DeVoe and Kistiakowsky, 1961), so that HCO 3 − > CO2 in the carboxysome.
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Prior to the addition of TdT enzyme, sections were deparaffinized with xylene and rehydrated through graded alcohol washes.
The purified enzyme catalyzes the uncoupled reductive cleavage of SAM in the absence of substrate, as has been observed for other radical SAM enzymes (section 2.3).
The idea has only recently been put forth that the oxidative dehydrogenation reactions catalyzed by enzymes like BtrN and anSME occur via reduction of the [4Fe 4S]2+ auxiliary clusters bound to these enzymes (section 8).
The two iron sulfur clusters and the enzyme active site were all found within a TIM barrel fold, and the authors pointed out the intriguing similarity between the biotin synthase structure and those of AdoCbl radical enzymes (section 2.7).
With the recent in vitro characterization of cobalamin-containing class B radical SAM methyltransferase enzymes (section 7.1), in vitro characterization of BchE should provide insight into the diversity that the cobalamin serves in the radical SAM-initiated mechanism expected by BchE.
The methodology of the assay is described in enzyme assay section.
The activities of MnP and Lac from C. basilensis B-8 have been observed using colorimetric enzyme assays (Section "Analysis of enzymes related to KL degradation").
For immunohistochemistry with alkaline phosphatase as the enzyme system, sections were blocked with 20% acetic acid for 20 minutes at 4°C.
Mutations in SUMF1 cause multiple sulfatase deficiency, a rare and fatal autosomal recessive disorder characterized by absent activity of all sulfatase enzymes (see Section V.A) (40, 41).
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