What substrate is used in the Bowers-McComb method for measuring ALP?

The Bowers-McComb method for measuring alkaline phosphatase (ALP) specifically employs alpha-naphthylphosphate as the substrate. This method is based on the enzyme's ability to hydrolyze this substrate, leading to the release of alpha-naphthol, which can then be measured quantitatively.

In this method, the released alpha-naphthol reacts with a diazonium compound, resulting in a colored compound that can be measured photometrically, allowing for the quantification of alkaline phosphatase activity in a sample.

The other substrates mentioned, such as beta-glycerophosphate and p-nitrophenylphosphate, are used in different methods for measuring ALP activity but are not the specific substrates utilized in the Bowers-McComb approach. Each substrate used for ALP measurement can result in different levels of sensitivity and specificity in detecting enzyme activity, which underscores the importance of using the correct substrate for accurate measurement.