TY - JOUR
T1 - Demonstration of Acid Phosphatase in Eimeria spp.
T2 - Partial Characterization of the Enzyme in E. vermiformis,
AU - HOSEK, JAMES E.
AU - TODD, KENNETH S.
AU - KUHLENSCHMIDT, MARK S.
N1 - Copyright:
Copyright 2016 Elsevier B.V., All rights reserved.
PY - 1988/11
Y1 - 1988/11
N2 - 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 sporubted oocysts, that the enzyme is resistant to inhibition by tartrate, and that it can be separated into two forms by anion exchange chroma‐tography.
AB - 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 sporubted oocysts, that the enzyme is resistant to inhibition by tartrate, and that it can be separated into two forms by anion exchange chroma‐tography.
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U2 - 10.1111/j.1550-7408.1988.tb04145.x
DO - 10.1111/j.1550-7408.1988.tb04145.x
M3 - Article
C2 - 3199338
AN - SCOPUS:0024118084
SN - 1066-5234
VL - 35
SP - 531
EP - 532
JO - Journal of Protozoology
JF - Journal of Protozoology
IS - 4
ER -