Studies on American Paragonimiasis. III. Phosphomonoesterase Activity

Abstract

Acid and alkaline phosphomonoesterase activity has been studied in Paragonimus kellicotti Ward, 1908. The enzymes have been partially purified by differential centrifugation and column chromatography on P-60 polyacrylamlde gel. These steps also removed endogenous inorganic phosphate which allowed subsequent reactions to be completed at zero-order kinetics. The partially purified enzymes exhibited maximal activity at pH 4.5 and 9.0 against a variety of substrates. In addition, three other substrates were hydrolyzed at a maximal rate at other pH values. These included glucose-6-phosphate at 6,8, AMP at 7.2, and fructose-1, 6-diphosphate at 10.0. These data inaicate that a complex group of enzymes are involved in the breakdown of phosphomonoesterases by Paragonimus kellicotti.