Activation of porcine heart mitochondrial malate dehydrogenase by zero valence sulfur and rhodanese

Incubation of malate dehydrogenase with thiosulfate and rhodanese lead to an increase of dehydrogenasic activity. Selenosulfate, elemental sulfur and elemental selenium were shown similarly able to activate this protein. The activation is limited to the presence of SH groups on the protein. Experime...

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Published inBiochemical and biophysical research communications Vol. 68; no. 2; pp. 553 - 560
Main Authors Finazzi Agrò, Alessandro, Mavelli, Irene, Cannella, Carlo, Federici, Giorgio
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.01.1976
Subjects
animal science
Enzyme Activation - drug effects
Kinetics
livestock
Malate Dehydrogenase - metabolism
Mitochondria, Muscle - enzymology
Myocardium
Sulfur - pharmacology
Sulfurtransferases - pharmacology
Thiosulfate Sulfurtransferase - pharmacology
Thiosulfates - pharmacology
zoology
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Summary:Incubation of malate dehydrogenase with thiosulfate and rhodanese lead to an increase of dehydrogenasic activity. Selenosulfate, elemental sulfur and elemental selenium were shown similarly able to activate this protein. The activation is limited to the presence of SH groups on the protein. Experiments with 35S demonstrated the direct transfer of zero valence sulfur from rhodanese to malate dehydrogenase. It is proposed that this activation could be a mechanism of enzyme activity modulation in vivo.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(76)91181-5