Purification and partial characterization of arylsulphatase C from human placental microsomes.
Arylsulphatase C (EC 3.1.6.1) has been purified 300-fold from human placental microsomes using a four step procedure involving solubilization with Triton X-100, chromatography on hydroxyapatite, column chromatofocussing and ion-exchange chromatography on DEAE-Sepharose. The purified enzyme is electrophoretically homogeneous and has a molecular weight of 440 000 as determined by polyacrylamide gradient gel electrophoresis. On analysis of the preparation by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate a polypeptide of molecular weight 74 000 was observed, suggesting that the enzyme as purified may be a hexamer. The behaviour of the enzyme during chromatofocussing indicates the enzyme has a pI of 6.56. Steroid sulphatase, as measured by activity towards dehydroepiandrosterone sulphate, co-purifies with arylsulphatase C suggesting that both activities are due to a single enzyme.
D000818:Animals; D001192:Arylsulfatases / Q000302:isolation & purification* / Q000378:metabolism; D002458:Cell Fractionation; D005260:Female; D006801:Humans; D007700:Kinetics; D008861:Microsomes / Q000201:enzymology*; D008862:Microsomes, Liver / Q000201:enzymology; D008970:Molecular Weight; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D051381:Rats; D043266:Steryl-Sulfatase; D013429:Sulfatases / Q000302:isolation & purification*
D013429:Sulfatases; D001192:Arylsulfatases; D043266:Steryl-Sulfatase