Demonstration of acid phosphatase in Eimeria spp.: partial characterization of the enzyme in E. vermiformis.
Sporozoite extracts of E. vermiformis, E. stiedai, and E. tenella are rich in acid phosphatase activity. They contain specific enzyme activities equal to or greater than those reported for other highly virulent protozoan parasites. The absolute amount of enzyme activity per oocyst dramatically increases during sporulation of E. stiedai and E. vermiformis. Partial characterization of the acid phosphatase activity of E. vermiformis indicates that sporozoites account for greater than 92% of the total activity in sporulated oocysts, that the enzyme is resistant to inhibition by tartrate, and that it can be separated into two forms by anion exchange chromatography.
Hosek
J E
JE
Department of Pathobiology, College of Veterinary Medicine, University of Illinois, Urbana 61801.
Todd
K S
KS
Kuhlenschmidt
M S
MS
D000135:Acid Phosphatase / Q000378:metabolism*; D000818:Animals; D002852:Chromatography, Ion Exchange; D004539:Eimeria / Q000201:enzymology* / Q000502:physiology; D006867:Hydrolases / Q000378:metabolism; D012995:Solubility; D013045:Species Specificity; D013170:Spores
D006867:Hydrolases; D000135:Acid Phosphatase