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Abstract
2+ The effect of varying Mg levels on the enzymatic activity of bovine intestinal mucosa alkaline phosphatase in two different buffers was investigated. The maximum rates of bovine intestinal mucosa alkaline phosphatase enzymatic activity were determined by conducting a series of enzyme assays using p-nitrophenol phosphate as a substrate. Our 2+ observations determined that increasing the concentration of Mg in Tris-HCl buffer initially increased enzyme activity until a plateau was reached; whereas V continued to max 2+ increase in Tris-phosphate buffer within the range of Mg levels tested. A corresponding decrease and leveling off of K was observed in Tris-HCl buffer. A continual decrease in K m m 2+ in Tris-phosphate buffer was observed, suggesting that an increase in concentration of Mg 2+ increased the affinity of the enzyme for the pNPP substrate. A higher Mg concentration in the buffer may have helped the ion overcome the complexing effects of P in the Trisi phosphate buffer and improved its access to the enzyme. As a result, the rate of the enzyme reaction increased and a gradual stabilization of the enzyme was observed.