In the present study, the synthesis of Mg-Al layered double hydroxide at the molar ratio of 3:1 for Mg/Al are determined. One-step hydrothermal technique with slow hydrolysis of urea at a low temperature was employed without further annealing. The study was aimed at determining the effectiveness of Congo Red dye removal in the adsorption process onto Mg-Al layered double hydroxide (LDH) with respect to the change in pH of the solution. The experiment was conducted at concentrations of a sorbent 0.04g with 100 ml of Congo Red and at six values of the reaction, i.e. pH 2.0, pH 4.0, pH 6.0, pH 8.0, pH 10, and pH 12.0. It was found that pH affects the adsorbent surface charge and the degree of anionic dye dissociation. This can be explained to the chemical form of dye in the solution and functional groups present on the adsorbent surface at a specific pH.
Human acetyl‐coenzyme A carboxylase 2 catalyzes the carboxylation of acetyl coenzyme A to form malonyl coenzyme A, along with the conversion of magnesium‐adenosine triphosphate complex to magnesium‐adenosine diphosphate complex. A simple off‐column capillary electrophoresis assay for human acetyl‐coenzyme A carboxylase 2 was developed based on the separation of magnesium‐adenosine triphosphate complex, magnesium‐adenosine diphosphate complex, acetyl coenzyme A and malonyl coenzyme A with detection by ultraviolet absorption at 256 nm. When Mg2+ was absent from the separation buffer, the zones due to magnesium‐adenosine triphosphate complex and magnesium‐adenosine diphosphate complex both split and migrated as two separate peaks. With Mg2+ added to the separation buffer, magnesium‐adenosine triphosphate complex and magnesium‐adenosine diphosphate complex produced single peaks, and the reproducibility of peak shape and area improved for human acetyl‐coenzyme A carboxylase 2 assay components. The final separation buffer used was 30.0 mM HEPES, 3.0 mM MgCl2, 2.5 mM KHCO3, and 2.5 mM potassium citrate at pH 7.50. The same buffer was used for the enzyme‐catalyzed reaction (off‐column). Inhibition of human acetyl‐coenzyme A carboxylase 2 by CP‐640186, a known inhibitor, was detected using the capillary electrophoresis assay.
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