Phosphatases in helminths: Effects of pH and various chemicals and anthelmintics on the enzyme activities

Abstract

Phosphatases of four helminth species, Ascaridia galli, Centrorhynchus convi, Cotylophoron cotylophorum and Raillietina cesticillus have been analysed colorimetrically. The optimum pH for acid phosphatase activity was 5.4, 4.5, 4.7 and 5.0 in A. galli, C. convi, R. cesticillus and C. cotylophorum, respectively. The optimum pH for alkaline phosphatase activity was 9.1, 9.5, 8.7 and 8.4 in A. galli, C. corvi, R. cesticillus and C. cotylophorum, respectively. In A. galli and C. cotylophorum the acid phosphatase showed more activity than alkaline phosphatase, whereas the latter was more active in R. cesticillus and C. corvi. Effects of the various chemicals MgSO 4, CuSO 4, FeCl 3, KCN, NaF, sodium citrate, glycine and formaldehyde on the enzyme activities were studied. Variable degrees of inhibition of the enzyme activities were achieved following the addition of the anthelmintics Bilevon, Mansonil, Vermex, Zanil, Distodin and Carbon tetrachloride.