Abstract
The alkaline phosphomonoesterase activity of mitochondrial, microsomal, and soluble fractions prepared from Phormia regina (Meigen) were investigated, and the enzymes were partially purified. The alkaline phosphomonoesterases of these cell fractions are similar in pH optimum, metal ion activation, and stability in the presence and absence of substrate. Minor differences exist in the Michaelis constants, when p -nitrophenyl is used as the substrate, and in their substrate specificity. Manganese and magnesium are the most effective activators of several tested, and, in contrast to the corresponding enzymes in vertebrates, neither copper nor organic sulfhydryl binding agents are effective inhibitors.
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