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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1979-5-16
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pubmed:abstractText |
Dehydro-digitoxosides are metabolites of digitalis glycosides. In order to study their possible biological activity their affinity to (Na+ + K+)-activated ATPase was determined and compared with unchanged glycosides. Based on the dissociation constants of glycoside-enzyme-complexes, the affinity of the dehydro-digitoxosides ranged in the same order of magnitude as that of the native glycosides. Comparing mono-, bis-, and tris-digitoxosides of digitoxigenin (dt-1, dt-2, dt-3) and of digoxin (dg-1, dg-2, dg-3) with the corresponding dehydrodigitoxosides (3'-dehydro-dt-1, 9'-dehydro-dt-2, 15'-dehydro-dt3, 3'-dehydro-dg-1 and 9'-dehydro-dg-2, respectively) the dehydro-digitoxosides had lower affinities to the enzyme. The highest dissociation constants (KD) were found for 3'-dehydro-dt-1 and 3'-dehydro-dg-1. The half maximal inhibition of (Na+ + K+)-ATPase activity (I50) coresponded to affinity measurements in all but two cases: dehydro-dt-3 and dehydro-dt-2 showed very low I50 values.
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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/Digoxigenin,
http://linkedlifedata.com/resource/pubmed/chemical/Digoxin,
http://linkedlifedata.com/resource/pubmed/chemical/Ouabain,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Potassium-Exchanging ATPase
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0028-1298
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
306
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11-5
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pubmed:dateRevised |
2010-3-12
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pubmed:meshHeading |
pubmed-meshheading:218119-Animals,
pubmed-meshheading:218119-Biotransformation,
pubmed-meshheading:218119-Cattle,
pubmed-meshheading:218119-Digitoxigenin,
pubmed-meshheading:218119-Digoxigenin,
pubmed-meshheading:218119-Digoxin,
pubmed-meshheading:218119-Kinetics,
pubmed-meshheading:218119-Myocardium,
pubmed-meshheading:218119-Ouabain,
pubmed-meshheading:218119-Sodium-Potassium-Exchanging ATPase,
pubmed-meshheading:218119-Time Factors
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pubmed:year |
1979
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pubmed:articleTitle |
Dehydro-digitoxosides of digitoxigenin and digoxigenin: binding to beef heart (Na+ + K+)-ATPase in relation to unchanged digitoxosides.
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pubmed:publicationType |
Journal Article,
In Vitro
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