Abstract
The effect of magnesium ions on the catalytic activity of alkaline phosphatases from three different sources in the reaction of p-nitrophenyl phosphate hydrolysis was studied. It was found that magnesium in concentrations of 0.6 ng/mL-20 µg/mL significantly activated alkaline phosphatase from chicken intestine; in higher concentrations (0.02–0.2 mg/mL), it weakly activated the enzyme from E. coli and had no effect on the catalytic activity of the enzyme from the small intestine of the Greenland seal. The strongest activating effect was observed in a Tris-HCl buffer solution at pH 9.8. The activating effect of magnesium on alkaline phosphatase from chicken intestine was used as the basis for developing a highly sensitive and selective enzymatic procedure for determining magnesium (0.6–6.0 ng/mL; RSD = 4% at cmin; n = 5) by spectrophotometrically monitoring the rate of enzymatic reaction. The developed procedure was applied to the determination of magnesium in urine.
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