Linked Life Data

1796709

Source:http://linkedlifedata.com/resource/pubmed/id/1796709

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-4-9
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0001-527X
pubmed:author
pubmed:issnType
Print
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7-16
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Oestrone sulphate sulphohydrolase activity in nuclear envelopes from human placenta cell nuclei.
pubmed:affiliation
Department of Biochemistry, Nicolaus Copernicus University, Toru?, Poland.
pubmed:publicationType
Journal Article