Isolation and characterization of the pig endometrial arylsulphatase A.
The pig endometrial arylsulphatase A was purified 3322-fold to a specific activity of 150 mumol/min per mg. The purification involved (NH4)2SO4 fractionation, chromatography on concanavalin A-Sepharose and DEAE-Sepharose, gel filtrations on Sephadex G-200 at pH 7.4 and 5, and a new preparative gel-electrophoresis technique. The homogeneous enzyme is a glycoprotein containing 20% carbohydrate. The purified enzyme has Mr about 120 000 and it contains subunits of Mr 63 000. The pig endometrial arylsulphatase A shows many properties in common with those of arylsulphatases A purified from other sources. The similarities include their low isoelectric points, the anomalous time-activity relationships, multi-pH optima, inhibition by SO3(2-), SO4(2-), phosphate ions, metal ions and nucleoside phosphates, pH- and ionic-strength-dependent polymerization and amino acid composition.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002553:Cerebroside-Sulfatase / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D004717:Endometrium / Q000201:enzymology*; D004800:Enzymes, Immobilized; D005260:Female; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008970:Molecular Weight; D013379:Substrate Specificity; D013429:Sulfatases / Q000302:isolation & purification; D013552:Swine
D000596:Amino Acids; D004800:Enzymes, Immobilized; D013429:Sulfatases; D002553:Cerebroside-Sulfatase