An impurity in the buffer 2-amino-2-methyl-1-propanol, which correlates with depression of measured alkaline phosphatase activity.

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Abstract
Recent findings indicate that the buffer 2-amino-2-methyl-1-propanol, widely used in clinical measurement of alkaline phosphatase activity, contains an impurity that inhibits the activity of the enzyme. Analysis of several lots of 2-amino-2-methyl-1-propanol has demonstrated the presence of a material, the concentration of which correlates well with alkaline phosphatase activity. Mass spectral analysis of this material indicates that it is a substituted ethylenediamine compound. Zinc chelation is discussed as a possible mode of its inhibition. Further work is in progress to separate and characterize this and other compounds in the buffer and to determine their modes and degrees of alkaline phosphatase inhibition.