Comparison of arylsulphatases from Eimeria tenella (parasite) and chicken caecum (host).

Chicken caecal arylsulphatase was purified 700-fold by (NH4)2SO4 fractionation, concanavalin A-Sepharose and cyclic AMP-Sepharose chromatographies. The purified enzyme was a glycoprotein of Mr 97,000. It hydrolysed p-nitrocatechol sulphate, cerebroside 3-sulphate and ascorbic acid 2-sulphate and was strongly inhibited by Na2SO4 (Ki = 50 microM) and Na3PO4 (Ki = 20 microM). Arylsulphatase from Eimeria tenella sporozoites was purified 28-fold by (NH4)2SO4 fractionation. Arylsulphatase of E. tenella sporozoites was not a glycoprotein. It had an Mr of 49,000. It was inhibited by Na2SO4 (Ki = 300 microM), sodium phosphate (Ki = 90 microM) and heparin. It hydrolysed ascorbic acid 2-sulphate, but cerebroside 3-sulphate was not desulphated. The kinetic parameters of chicken caecal arylsulphatase were different from those of the E. tenella enzyme.