Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1990-3-1
pubmed:abstractText
Previous investigations on the digitoxin metabolism hardly considered the role of the sulfate ester conjugation. Therefore, this study examined whether digitoxin (dt-3) or one of its cleavage products might be sulfated in vitro. It was proven that digitoxigenin (dt-0) is by far the best substrate for the cytosolic sulfotransferases (ST). Digitoxigenin-monodigitoxoside (dt-1) and digitoxigenin-bisdigitoxoside (dt-2) are sulfated in trace amounts whereas dt-3 is not sulfated at all. The purification of the responsible enzyme was performed by liquid chromatography on Q-Sepharose and hydroxyapatite. During the purification procedure this enzymatic activity corresponded exactly to that towards dehydroepiandrosterone (DHEA). The 134-fold purified and gel electrophoretically homogeneous enzyme protein (Mr 33,000) showed a Vmax of 12.5 nmoles dt-0 sulfate/min mg protein and a KM of 37 mumol/L. The purified enzyme conjugated dt-1 and dt-2 in trace amounts only and was inhibited competitively by DHEA. It can be concluded that in the rat a 3 beta-hydroxy-steroid sulfotransferase is responsible for the sulfation of dt-0. The purified enzyme reacts with dt-1, dt-2 and digoxigenin (dg-0) in traces only, a sulfation of dt-3 is not detectable.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2952
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
301-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Purification of a rat liver cytosolic sulfotransferase responsible for the conjugation of digitoxigenin.
pubmed:affiliation
Institute for Legal Medicine, University of Hamburg, Federal Republic of Germany.
pubmed:publicationType
Journal Article, Comparative Study