Studies on American Paragonimiasis. III. Phosphomonoesterase Activity
- 1 April 1966
- journal article
- research article
- Published by JSTOR in Journal of Parasitology
- Vol. 52 (2) , 363-+
- https://doi.org/10.2307/3276501
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.This publication has 4 references indexed in Scilit:
- Studies on American Paragonimiasis. I. Age Immunity of the Snail HostJournal of Parasitology, 1965
- Acid Phosphatase in Clonorchis sinensisJournal of Parasitology, 1964
- MULTIPLE FORMS OF ENZYMES: TISSUE, ONTOGENETIC, AND SPECIES SPECIFIC PATTERNSProceedings of the National Academy of Sciences, 1959
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951