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The kinetic analysis of compound 6t revealed it inhibited α-glucosidase in an irreversible and mixed manner.
It was observed that the solder joints broke in a ductile manner at low strain rates (5 × 10−4 s−1, 5 × 10−3 s−1), although they exhibited a ductile-brittle mixed manner at intermediate (2 × 10−2 s−1) and a brittle manner at high strain rates (1 × 10−1 s−1, 2 × 10−1 s−10−1
The chip formation in this extrusion-shear mixed manner is sensitive to the location of the thin amorphous layer because there is no shear except for in the model-6.
Oxamate inhibited the catalytic reactions of FNLDH competitively with pyruvate, and the PALDH reaction in a mixed manner at pH 7.0, but markedly enhanced the reactions of the two enzymes at low concentration through canceling of the apparent homotropic cooperativity at pH 8.0, although it constantly inhibited the ECLDH reaction.
Oxamate, an inert pyruvate analogue, inhibited the reactions of the three enzymes at pH 7.0, where the enzymes showed no marked homotropic cooperativity, in different manners, i.e. an apparently competitive manner with pyruvate for FNLDH, and a mixed manner for PALDH and ECLDH (Figure 4).
In order to reduce confounding factors by performing these two tasks in a mixed manner, we separated the physical and social sessions.
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Surprisingly, despite significant shear band plasticity at 77 K, failure occurs in a mixed mode manner, with large areas showing quasi-cleavage features that appear to initiate from cracks at the glass-Ti interfaces, which also limit the overall plastic strain.
The maximal rate of uptake also decreases as the inhibitor concentration increases, which would not be expected for a purely competitive inhibitor suggesting that these compounds may be acting in a mixed competitive/noncompetitive manner.
We found that the reversible inhibition of tyrosinase by validamycin A occurred in a mixed-type manner with Ki = 5.893 ± 0.038 mM, as determined by integrating kinetics studies and computational simulations.
The results of a mixed-type manner in enzyme kinetic experiment and molecular docking study for 2-((diethylamino methyl -1-hydroxy-3- 3-methylbut-2-enyloxy -9H-xanthen-9-one diethylamino methyl -1-hydroxy-3- 3-methylbut-2-enyloxy -9H-xanthen-9-one active site (AS) andiethylamino methyl -1-hydroxy-3- 3-methylbut-2-enyloxy -9H-xanthen-9-one
Moreover, the compounds with alkyl substitutions in the position 3 of 1,3-dihydroxyxanthone showed higher potent inhibitory activities compared to 1a ~ 1e compounds with hydroxy in the position 3. Kinetic analysis suggested that the the Mannich base compound inhibited both cholinesterases in mixed-type manners, suggesting they might simultaneously interact with the AS and PAS of both enzymes.
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