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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1990-3-1
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Digitoxigenin,
http://linkedlifedata.com/resource/pubmed/chemical/Digitoxin,
http://linkedlifedata.com/resource/pubmed/chemical/Digoxigenin,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfotransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfurtransferases,
http://linkedlifedata.com/resource/pubmed/chemical/alcohol sulfotransferase
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-2952
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
39
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
301-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2302255-Animals,
pubmed-meshheading:2302255-Chromatography, Ion Exchange,
pubmed-meshheading:2302255-Cytosol,
pubmed-meshheading:2302255-Digitoxigenin,
pubmed-meshheading:2302255-Digitoxin,
pubmed-meshheading:2302255-Digoxigenin,
pubmed-meshheading:2302255-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2302255-Female,
pubmed-meshheading:2302255-Kinetics,
pubmed-meshheading:2302255-Liver,
pubmed-meshheading:2302255-Rats,
pubmed-meshheading:2302255-Rats, Inbred Strains,
pubmed-meshheading:2302255-Sulfotransferases,
pubmed-meshheading:2302255-Sulfurtransferases
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pubmed:year |
1990
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pubmed:articleTitle |
Purification of a rat liver cytosolic sulfotransferase responsible for the conjugation of digitoxigenin.
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pubmed:affiliation |
Institute for Legal Medicine, University of Hamburg, Federal Republic of Germany.
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pubmed:publicationType |
Journal Article,
Comparative Study
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