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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1985-11-14
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pubmed:abstractText |
Dinucleosidetriphosphatase (EC 3.6.1.29) is present in both the 37,000 g rat liver supernatant and precipitate (50 mU/g each fraction). These two activities show matching molecular weights, isoelectric points, substrate specificities, Km values, bivalent cation requirements and inhibition by zinc (II). The particulate triphosphatase and a residual dinucleosidetetraphosphatase (EC 3.6.1.17) are solubilized by freeze-thawing or by Triton X-100. Detergent treatment also extracts an unspecific phosphodiesterase I activity (EC 3.1.4.1) which also splits dinucleoside polyphosphates. The above findings suggest the occurrence of cytosolic and particulate degradative pathways for dinucleoside polyphosphates.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0020-711X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
903-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2995162-Animals,
pubmed-meshheading:2995162-Cytosol,
pubmed-meshheading:2995162-Hydrolysis,
pubmed-meshheading:2995162-Kinetics,
pubmed-meshheading:2995162-Liver,
pubmed-meshheading:2995162-Molecular Weight,
pubmed-meshheading:2995162-Nucleoside-Triphosphatase,
pubmed-meshheading:2995162-Phosphoric Monoester Hydrolases,
pubmed-meshheading:2995162-Rats,
pubmed-meshheading:2995162-Substrate Specificity
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pubmed:year |
1985
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pubmed:articleTitle |
Occurrence of dinucleosidetriphosphatase in the cytosol and particulate fractions from rat liver.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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