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

Abstract

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.

Structural insights into choline-O-sulfatase reveal the molecular determinants for ligand binding

“…Sulfate binding. The inhibition of the phosphatase superfamily by secondary products (sulfate and phosphate) has been well documented (Farooqui & Hanson, 1987;Ueki et al, 1995;. Sulfate slightly decreased the activity of the partially purified Aspergillus and Penicillium COSe enzymes Segel & Johnson, 1963), but was reported not to inhibit Pseudomonas COSe (up to 30 mM; Takebe, 1961) 3a and 4a), most likely arising from the high concentrations of sulfate used in the crystallization conditions (1 M ammonium sulfate; Supplementary Fig.…”