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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
1981-4-21
|
| pubmed:abstractText |
A Ca/+-activated protease from rat liver cell sap was prepared. It was shown to act on rat liver pyruvate kinase that had been phosphorylated by the catalytic subunit of cyclic AMP-dependent protein kinase, the activity being optimum at neutral pH. The modified pyruvate kinase had the same Vmax as the phosphoenzyme but showed a lower affinity for the substrate phosphoenolpyruvate. The possibility that this proteolytic attack is the step that initiates further degradation in the cell is discussed.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0302-4369
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
34
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
419-22
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7008473-Animals,
pubmed-meshheading:7008473-Calcium,
pubmed-meshheading:7008473-Hydrogen-Ion Concentration,
pubmed-meshheading:7008473-Kinetics,
pubmed-meshheading:7008473-Liver,
pubmed-meshheading:7008473-Peptide Hydrolases,
pubmed-meshheading:7008473-Phosphorylation,
pubmed-meshheading:7008473-Pyruvate Kinase,
pubmed-meshheading:7008473-Rats
|
| pubmed:year |
1980
|
| pubmed:articleTitle |
The in vitro modification of phosphorylated pyruvate kinase by a Ca2+-activated protease from rat liver.
|
| pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|