Abstract
The enzyme for dephosphorylation of FMN was purified from the mucosa of dog's small intestine. From the results obtained on optimum pH, optimum temperature, and substrate specificity of the enzyme, and on the rate of purification of the enzyme for dephosphorylation of both FMN and β-glycerophosphate, it is considered that the enzyme is identical with intestinal alkaline phosphomonoesterase.