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.
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Research Article| June 01 1983
Isolation and characterization of the pig endometrial arylsulphatase A.
Biochem J (1983) 211 (3): 649–659.
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H Rahi, P N Srivastava; Isolation and characterization of the pig endometrial arylsulphatase A.. Biochem J 1 June 1983; 211 (3): 649–659. doi: https://doi.org/10.1042/bj2110649
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