Oestrone sulphate sulphohydrolase activity in nuclear envelopes from human placenta cell nuclei.
Procedures for isolation, from human term placenta, of highly purified nuclei and nuclear envelopes with a low content of DNA are described. Both fractions contain oestrone sulphate sulphohydrolase activity. The enzyme from nuclear envelopes can be solubilized with Triton X-100 and, partially, with proteolytic enzymes. It does not require Ca2+ and is insensitive to Ag+ and agents reacting with SH groups. It is strongly inhibited by millimolar concentrations of sulphites and to a much smaller extent by phosphates. Oxidized forms of ascorbic acid, glutathione and NAD+ revealed a pronounced inhibitory effect, whereas reduced forms of these compounds produced a slight activation. It is proposed that oestrone sulphate sulphohydrolase activity in nuclear envelopes from human placenta is not exerted by arylsulphatase but represents a specific enzyme.
Gniot-Szulzycka
J
J
Department of Biochemistry, Nicolaus Copernicus University, Toruń, Poland.
Jakubowska
A
A
D001192:Arylsulfatases / Q000378:metabolism*; D002467:Cell Nucleus / Q000187:drug effects / Q000201:enzymology*; D010450:Endopeptidases; D006801:Humans; D006868:Hydrolysis; D009685:Nuclear Envelope / Q000187:drug effects / Q000201:enzymology*; D010084:Oxidation-Reduction; D010920:Placenta / Q000187:drug effects / Q000201:enzymology*; D043266:Steryl-Sulfatase; D013439:Sulfhydryl Reagents
D013439:Sulfhydryl Reagents; D001192:Arylsulfatases; D043266:Steryl-Sulfatase; D010450:Endopeptidases