Bacterial alkaline phosphatase applications

This section focuses on two most widely used APases, a bacterial alkaline phosphatase (BAP) from E. coli and a mammalian APase from calf intestinal mucosa (CIAP), to illustrate various strategies common to the application of APases. For the sake of general information on the diversity of mammalian APases, a brief description is given for human APases. 

Enzymes modified with carbohydrates (neoglycoenzymes) can be used in cytochemistry as described above or in biochemical detection of lectins in solid-phase assays to gain greater sensitivity in analysis. For example, bacterial 3-galactosidase modified with p-aminophenyl a-D-mannopyranoside via amide linkage was useful in determination of Con A immobilized on plastic microtiter plates, and lactose-modified P-galactosidase was effective in histochemical detection of galactoside-specific lectins [63]. Other enzymes frequently used for these applications are alkaline phosphatase and horse radish peroxidase. There are a number of colorimetric, fluorometric, and chemiluminescent substrates available for these enzymes. 

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